The C Terminus of Annexin II Mediates Binding to F-actin

Annexin II heterotetramer (AIIt) is a multifunctional Ca2+-binding protein composed of two 11-kDa subunits and two annexin II subunits. The annexin II subunit contains the binding sites for anionic phospholipids, heparin, and F-actin, whereas the p11 subunit provides a regulatory function. The F-actin-binding site is presently unknown. In the present study we have utilized site-directed mutagenesis to create annexin II mutants with truncations in the C terminus of the molecule. Interestingly, a mutant annexin II lacking its C-terminal 16, 13, or 9 amino acids was unable to bind to F-actin but still retained its ability to interact with both anionic phospholipids and heparin. Recombinant AIIt, composed of wild-type p11 subunits and the mutant annexin II subunits, was also unable to bundle F-actin. This loss of F-actin bundling activity was directly attributable to the inability of mutant AIIt to bind F-actin. These results establish for the first time that the annexin II C-terminal amino acid residues, LLYLCGGDD, participate in F-actin binding. Annexin II heterotetramer (AIIt) is a multifunctional Ca2+-binding protein composed of two 11-kDa subunits and two annexin II subunits. The annexin II subunit contains the binding sites for anionic phospholipids, heparin, and F-actin, whereas the p11 subunit provides a regulatory function. The F-actin-binding site is presently unknown. In the present study we have utilized site-directed mutagenesis to create annexin II mutants with truncations in the C terminus of the molecule. Interestingly, a mutant annexin II lacking its C-terminal 16, 13, or 9 amino acids was unable to bind to F-actin but still retained its ability to interact with both anionic phospholipids and heparin. Recombinant AIIt, composed of wild-type p11 subunits and the mutant annexin II subunits, was also unable to bundle F-actin. This loss of F-actin bundling activity was directly attributable to the inability of mutant AIIt to bind F-actin. These results establish for the first time that the annexin II C-terminal amino acid residues, LLYLCGGDD, participate in F-actin binding. ezrin-radixin-moesin family of proteins bovine serum albumin annexin II tetramer 11-kDa light chain of annexin II tetramer recombinant AIIt composed of wild-type p11 subunit and wild-type annexin II subunit (Ser1-Asp338) recombinant AIIt composed of wild-type p11 subunit and mutant annexin II subunit (Ser1-Ala329) recombinant AIIt composed of wild-type p11 subunit and mutant annexin II subunit (Ser1-Asp325) recombinant AIIt composed of wild-type p11 subunit and mutant annexin II subunit (Ser1-Thr322) polyacrylamide gel electrophoresis dithiothreitol total ligand concentration for half-maximal response 4-morpholinepropanesulfonic acid The cortical region of eukaryotic cells is made up of the plasma membrane and the underlying protein meshwork of the cytoskeleton. The cortical cytoskeleton plays a role in phenomenon such as cellular morphology, membrane domain specialization, and cell-cell and cell-substratum interactions (1Hitt A.L. Luna E.J. Curr. Opin. Cell Biol. 1994; 6: 120-130Crossref PubMed Scopus (123) Google Scholar, 2Luna E.J. Hitt A.L. Science. 1992; 258: 955-964Crossref PubMed Scopus (691) Google Scholar). In addition, the cortical cytoskeleton is involved in signal transduction events that regulate membrane trafficking, cell migration, and growth regulation (3Yin H.L. Stull J.T. J. Biol. Chem. 1999; 274: 32529-32530Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar, 4Aspenstrom P. Exp. Cell Res. 1999; 246: 20-25Crossref PubMed Scopus (101) Google Scholar, 5Keely P.J. Westwick J.K. Whitehead I.P. Der C.J. Parise L.V. Nature. 1997; 390: 632-636Crossref PubMed Scopus (649) Google Scholar, 6Hotchin N.A. Hall A. Cancer Surv. 1996; 27: 311-322PubMed Google Scholar, 7Palmieri S.J. Nebl T. Pope R.K. Seastone D.J. Lee E. Hinchcliffe E.H. Sluder G. Knecht D. Cardelli J. Luna E.J. Cell Motil. Cytoskeleton. 2000; 46: 285-304Crossref PubMed Scopus (40) Google Scholar). A major portion of the cortical cytoskeleton is made up actin filaments whose physiological state is governed by actin-binding proteins. These actin-binding proteins control actin filament polymerization, filament-filament interaction, and filament-plasma membrane interaction (reviewed in Ref. 8Pollard T.D. Almo S. Quirk S. Vinson V. Lattman E.E. Annu. Rev. Cell Biol. 1994; 10: 207-249Crossref PubMed Scopus (86) Google Scholar).The proteins that link the actin cytoskeleton with the plasma membrane are particularly diverse in their actions. An example is the ezrin-radixin-moesin (ERM)1family of proteins (9Bretscher A. Curr. Opin. Cell Biol. 1999; 11: 109-116Crossref PubMed Scopus (330) Google Scholar). These proteins are known to be involved in cytoskeletal-membrane events such as cell adhesion (10Hiscox S. Jiang W.G. J. Cell Sci. 1999; 112: 3081-3090Crossref PubMed Google Scholar, 11Vaheri A. Carpen O. Heiska L. Helander T.S. Jaaskelainen J. Majander-Nordenswan P. Sainio M. Timonen T. Turunen O. Curr. Opin. Cell Biol. 1997; 9: 659-666Crossref PubMed Scopus (161) Google Scholar, 12Mangeat P. Roy C. Martin M. Trends Cell Biol. 1999; 9: 187-192Abstract Full Text Full Text PDF PubMed Scopus (340) Google Scholar), Rho- and Rac-mediated cell morphology (13Lamb R.F. Roy C. Diefenbach T.J. Vinters H.V. Johnson M.W. Hall A. Cell Biol. 2000; PubMed Scopus Google Scholar, D.J. Hall A. J. Cell Biol. 1997; PubMed Scopus Google Scholar, M. T. S. M. T. S. S. J. Cell Biol. 1996; PubMed Scopus Google Scholar, T. A. T. S. J. Biol. Chem. 1997; Full Text Full Text PDF PubMed Scopus Google as as cell A. P. D. M. Sci. S. A. 1999; PubMed Scopus Google Scholar). and of cortical actin-binding proteins be in the in that the eukaryotic cell and its binding the II is a of the annexin family of proteins that are by their ability to bind to phospholipids in a Cell PubMed Scopus Google Scholar). In to their binding family to bind F-actin in a S. PubMed Scopus Google Scholar). Annexin II is the in that as both a and a tetramer the Annexin II tetramer (AIIt) of two of annexin II to a of a of the family of Ca2+-binding proteins. the that annexin II is the whereas AIIt is to the plasma cytoskeleton 1997; PubMed Scopus Google Scholar, T. C. V. J. Cell Sci. Google Scholar, Biol. Res. Google Scholar, L. J. Cell Biol. PubMed Scopus Google Scholar). that AIIt as a link the cytoskeleton and the plasma the physiological of interaction are V. 1997; PubMed Scopus Google both annexin II and AIIt bind F-actin in AIIt F-actin J. Biol. Chem. Full Text PDF PubMed Google Scholar). The bundling of F-actin by AIIt was and and of (AIIt) of This was the of with half-maximal The region of annexin II that to the bundling activity of AIIt bundling activity was a region of in the domain of annexin II that to actin-binding site of J. Biol. Chem. 1992; Full Text PDF PubMed Google Scholar). region of annexin II was for the F-actin bundling activity of AIIt, participate in F-actin binding. In to the F-actin bundling domain of AIIt, the F-actin binding domain of annexin II we present that the C terminus of the annexin II subunit of AIIt F-actin binding Interestingly, the 9 amino acid of the C terminus of the annexin II subunit to be for the F-actin binding activity of II tetramer (AIIt) is a multifunctional protein that in a with anionic phospholipids, F-actin, and Cell PubMed Scopus Google Scholar). to its ability to bind to actin and phospholipids, is to cells as a protein V. 1997; PubMed Scopus Google Scholar). is that the annexin II subunit of the protein the binding sites for the as as the sites for Cell PubMed Scopus Google Scholar). the of the F-actin-binding sites the protein The in the proteins and AIIt, and the of the F-actin binding domain the C terminus of the to that the C-terminal region of the annexin II subunit of AIIt be involved in F-actin binding. is known that the terminus of annexin II is for binding of p11 L. J. Cell Biol. PubMed Scopus Google Scholar, Sci. S. A. PubMed Scopus Google Scholar, M. T. J. Biol. Chem. Full Text PDF PubMed Google Scholar), a role to the C-terminal region of the we have site-directed mutagenesis to the C terminus of annexin II to its in F-actin that of the amino acid of the C terminus of the annexin II subunit of AIIt the F-actin bundling activity of the protein by This to that the C terminus was involved in the interaction with F-actin. the F-actin binding activity of the annexin II of the F-actin binding of C-terminal truncations of annexin II that of or as as 9 amino acid also the F-actin binding activity of the the truncations in the C terminus of annexin II the interaction of annexin II with or heparin. The annexin II mutant proteins to and in a with a and as annexin mutant annexin II to a in a as annexin II to the annexin II to annexin II that was with we the ability of the AIIt, composed of wild-type p11 subunits and annexin II subunits to bundle F-actin AIIt composed of wild-type p11 subunits and annexin II subunits was unable to bundle F-actin. that the loss in F-actin bundling was to a in the binding of the mutant AIIt to results for the first time that the C-terminal of the annexin II subunit of AIIt, LLYLCGGDD, contains F-actin binding domain of The of the F-actin binding domain to the C-terminal 9 amino acid of annexin II of the F-actin binding to also contains a actin-binding In a region the first amino acid of the protein the actin-binding site J. C. Res. 1996; PubMed Scopus Google Scholar, M. D. M. J. C. J. 1996; PubMed Scopus Google Scholar). is a with a for F-actin D. J. J. D. J. Biol. Chem. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar, M. D. Res. 1999; PubMed Scopus Google Scholar, Curr. Opin. Cell Biol. PubMed Scopus Google Scholar). F-actin binding are in with the F-actin-binding sites of the proteins to amino acids D.J. Hall A. J. Cell Biol. 1997; PubMed Scopus Google Scholar, O. T. A. J. Cell Biol. 1994; PubMed Scopus Google Scholar). F-actin binding domain in amino acid of the protein P.J. Stull J.T. Cell 1997; PubMed Scopus Google Scholar). in light of the F-actin-binding sites of the the F-actin-binding site of is amino acid in M. P. M. G. J. Cell Biol. 1994; PubMed Scopus Google Scholar). In addition, the F-actin-binding sites the D. protein in to amino acid in the acid domain binding to F-actin S. M. 1999; PubMed Scopus Google the of the F-actin-binding site of annexin II is with known for F-actin binding site to be the of F-actin-binding sites are the C terminus of annexin is known that the of F-actin-binding sites of T.D. Almo S. Quirk S. Vinson V. Lattman E.E. Annu. Rev. Cell Biol. 1994; 10: 207-249Crossref PubMed Scopus (86) Google Scholar). Interestingly, the region of annexin II that we contains the F-actin-binding site known to be of A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google that a to the C-terminal amino acid of annexin II the binding of annexin II or AIIt to F-actin. we that the to the C-terminal amino acid of annexin II was unable to F-actin binding by annexin II or AIIt the that was to the C-terminal region of annexin was that was in the as the C-terminal region of annexin of a portion of with inability of a to the C-terminal amino acids of annexin II to directly bind to F-actin two is that the C-terminal 9 amino acid of annexin II be of the F-actin-binding site and amino acids residues, by of annexin participate in of the the C-terminal region of annexin II F-actin, is that the C terminus interaction with amino acids to a that C-terminal amino acid to bind F-actin. is to that the was unable to the the of amino acid of annexin II to its was also that the C-terminal truncations of annexin II the F-actin binding activity of AIIt with the annexin This was is AIIt and annexin II that to the F-actin cytoskeleton. the binding of the p11 subunit to annexin II the C-terminal region of annexin II in a that the 9 amino acid to the F-actin-binding In is that the for amino acids to the interaction of the 9 C-terminal amino acid with F-actin is by the binding of p11 to annexin is with of the F-actin-binding site of annexin II to the C is known that annexin II with and The of the is to the plasma membrane and is known to the Ca2+-binding sites and the binding A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google Scholar). The of the protein is to the and contains both the and C-terminal of the is that the terminus with p11 to AIIt, and the that the C terminus also the in to interact with the actin cytoskeleton the AIIt is its role as a the C-terminal domain of annexin II to be in the to bind to and the actin cytoskeleton. The cortical region of eukaryotic cells is made up of the plasma membrane and the underlying protein meshwork of the cytoskeleton. The cortical cytoskeleton plays a role in phenomenon such as cellular morphology, membrane domain specialization, and cell-cell and cell-substratum interactions (1Hitt A.L. Luna E.J. Curr. Opin. Cell Biol. 1994; 6: 120-130Crossref PubMed Scopus (123) Google Scholar, 2Luna E.J. Hitt A.L. Science. 1992; 258: 955-964Crossref PubMed Scopus (691) Google Scholar). In addition, the cortical cytoskeleton is involved in signal transduction events that regulate membrane trafficking, cell migration, and growth regulation (3Yin H.L. Stull J.T. J. Biol. Chem. 1999; 274: 32529-32530Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar, 4Aspenstrom P. Exp. Cell Res. 1999; 246: 20-25Crossref PubMed Scopus (101) Google Scholar, 5Keely P.J. Westwick J.K. Whitehead I.P. Der C.J. Parise L.V. Nature. 1997; 390: 632-636Crossref PubMed Scopus (649) Google Scholar, 6Hotchin N.A. Hall A. Cancer Surv. 1996; 27: 311-322PubMed Google Scholar, 7Palmieri S.J. Nebl T. Pope R.K. Seastone D.J. Lee E. Hinchcliffe E.H. Sluder G. Knecht D. Cardelli J. Luna E.J. Cell Motil. Cytoskeleton. 2000; 46: 285-304Crossref PubMed Scopus (40) Google Scholar). A major portion of the cortical cytoskeleton is made up actin filaments whose physiological state is governed by actin-binding proteins. These actin-binding proteins control actin filament polymerization, filament-filament interaction, and filament-plasma membrane interaction (reviewed in Ref. 8Pollard T.D. Almo S. Quirk S. Vinson V. Lattman E.E. Annu. Rev. Cell Biol. 1994; 10: 207-249Crossref PubMed Scopus (86) Google Scholar). The proteins that link the actin cytoskeleton with the plasma membrane are particularly diverse in their actions. An example is the ezrin-radixin-moesin (ERM)1family of proteins (9Bretscher A. Curr. Opin. Cell Biol. 1999; 11: 109-116Crossref PubMed Scopus (330) Google Scholar). These proteins are known to be involved in cytoskeletal-membrane events such as cell adhesion (10Hiscox S. Jiang W.G. J. Cell Sci. 1999; 112: 3081-3090Crossref PubMed Google Scholar, 11Vaheri A. Carpen O. Heiska L. Helander T.S. Jaaskelainen J. Majander-Nordenswan P. Sainio M. Timonen T. Turunen O. Curr. Opin. Cell Biol. 1997; 9: 659-666Crossref PubMed Scopus (161) Google Scholar, 12Mangeat P. Roy C. Martin M. Trends Cell Biol. 1999; 9: 187-192Abstract Full Text Full Text PDF PubMed Scopus (340) Google Scholar), Rho- and Rac-mediated cell morphology (13Lamb R.F. Roy C. Diefenbach T.J. Vinters H.V. Johnson M.W. Hall A. Cell Biol. 2000; PubMed Scopus Google Scholar, D.J. Hall A. J. Cell Biol. 1997; PubMed Scopus Google Scholar, M. T. S. M. T. S. S. J. Cell Biol. 1996; PubMed Scopus Google Scholar, T. A. T. S. J. Biol. Chem. 1997; Full Text Full Text PDF PubMed Scopus Google as as cell A. P. D. M. Sci. S. A. 1999; PubMed Scopus Google Scholar). and of cortical actin-binding proteins be in the in that the eukaryotic cell and its binding the Annexin II is a of the annexin family of proteins that are by their ability to bind to phospholipids in a Cell PubMed Scopus Google Scholar). In to their binding family to bind F-actin in a S. PubMed Scopus Google Scholar). Annexin II is the in that as both a and a tetramer the Annexin II tetramer (AIIt) of two of annexin II to a of a of the family of Ca2+-binding proteins. the that annexin II is the whereas AIIt is to the plasma cytoskeleton 1997; PubMed Scopus Google Scholar, T. C. V. J. Cell Sci. Google Scholar, Biol. Res. Google Scholar, L. J. Cell Biol. PubMed Scopus Google Scholar). that AIIt as a link the cytoskeleton and the plasma the physiological of interaction are V. 1997; PubMed Scopus Google Scholar). both annexin II and AIIt bind F-actin in AIIt F-actin J. Biol. Chem. Full Text PDF PubMed Google Scholar). The bundling of F-actin by AIIt was and and of (AIIt) of This was the of with half-maximal The region of annexin II that to the bundling activity of AIIt bundling activity was a region of in the domain of annexin II that to actin-binding site of J. Biol. Chem. 1992; Full Text PDF PubMed Google Scholar). region of annexin II was for the F-actin bundling activity of AIIt, participate in F-actin binding. In to the F-actin bundling domain of AIIt, the F-actin binding domain of annexin II we present that the C terminus of the annexin II subunit of AIIt F-actin binding Interestingly, the 9 amino acid of the C terminus of the annexin II subunit to be for the F-actin binding activity of II tetramer (AIIt) is a multifunctional protein that in a with anionic phospholipids, F-actin, and Cell PubMed Scopus Google Scholar). to its ability to bind to actin and phospholipids, is to cells as a protein V. 1997; PubMed Scopus Google Scholar). is that the annexin II subunit of the protein the binding sites for the as as the sites for Cell PubMed Scopus Google Scholar). the of the F-actin-binding sites the protein The in the proteins and AIIt, and the of the F-actin binding domain the C terminus of the to that the C-terminal region of the annexin II subunit of AIIt be involved in F-actin binding. is known that the terminus of annexin II is for binding of p11 L. J. Cell Biol. PubMed Scopus Google Scholar, Sci. S. A. PubMed Scopus Google Scholar, M. T. J. Biol. Chem. Full Text PDF PubMed Google Scholar), a role to the C-terminal region of the we have site-directed mutagenesis to the C terminus of annexin II to its in F-actin that of the amino acid of the C terminus of the annexin II subunit of AIIt the F-actin bundling activity of the protein by This to that the C terminus was involved in the interaction with F-actin. the F-actin binding activity of the annexin II of the F-actin binding of C-terminal truncations of annexin II that of or as as 9 amino acid also the F-actin binding activity of the the truncations in the C terminus of annexin II the interaction of annexin II with or heparin. The annexin II mutant proteins to and in a with a and as annexin mutant annexin II to a in a as annexin II to the annexin II to annexin II that was with we the ability of the AIIt, composed of wild-type p11 subunits and annexin II subunits to bundle F-actin AIIt composed of wild-type p11 subunits and annexin II subunits was unable to bundle F-actin. that the loss in F-actin bundling was to a in the binding of the mutant AIIt to results for the first time that the C-terminal of the annexin II subunit of AIIt, LLYLCGGDD, contains F-actin binding domain of The of the F-actin binding domain to the C-terminal 9 amino acid of annexin II of the F-actin binding to also contains a actin-binding In a region the first amino acid of the protein the actin-binding site J. C. Res. 1996; PubMed Scopus Google Scholar, M. D. M. J. C. J. 1996; PubMed Scopus Google Scholar). is a with a for F-actin D. J. J. D. J. Biol. Chem. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar, M. D. Res. 1999; PubMed Scopus Google Scholar, Curr. Opin. Cell Biol. PubMed Scopus Google Scholar). F-actin binding are in with the F-actin-binding sites of the proteins to amino acids D.J. Hall A. J. Cell Biol. 1997; PubMed Scopus Google Scholar, O. T. A. J. Cell Biol. 1994; PubMed Scopus Google Scholar). F-actin binding domain in amino acid of the protein P.J. Stull J.T. Cell 1997; PubMed Scopus Google Scholar). in light of the F-actin-binding sites of the the F-actin-binding site of is amino acid in M. P. M. G. J. Cell Biol. 1994; PubMed Scopus Google Scholar). In addition, the F-actin-binding sites the D. protein in to amino acid in the acid domain binding to F-actin S. M. 1999; PubMed Scopus Google the of the F-actin-binding site of annexin II is with known for F-actin binding site to be the of F-actin-binding sites are the C terminus of annexin is known that the of F-actin-binding sites of T.D. Almo S. Quirk S. Vinson V. Lattman E.E. Annu. Rev. Cell Biol. 1994; 10: 207-249Crossref PubMed Scopus (86) Google Scholar). Interestingly, the region of annexin II that we contains the F-actin-binding site known to be of A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google that a to the C-terminal amino acid of annexin II the binding of annexin II or AIIt to F-actin. we that the to the C-terminal amino acid of annexin II was unable to F-actin binding by annexin II or AIIt the that was to the C-terminal region of annexin was that was in the as the C-terminal region of annexin of a portion of with inability of a to the C-terminal amino acids of annexin II to directly bind to F-actin two is that the C-terminal 9 amino acid of annexin II be of the F-actin-binding site and amino acids residues, by of annexin participate in of the the C-terminal region of annexin II F-actin, is that the C terminus interaction with amino acids to a that C-terminal amino acid to bind F-actin. is to that the was unable to the the of amino acid of annexin II to its was also that the C-terminal truncations of annexin II the F-actin binding activity of AIIt with the annexin This was is AIIt and annexin II that to the F-actin cytoskeleton. the binding of the p11 subunit to annexin II the C-terminal region of annexin II in a that the 9 amino acid to the F-actin-binding In is that the for amino acids to the interaction of the 9 C-terminal amino acid with F-actin is by the binding of p11 to annexin is with of the F-actin-binding site of annexin II to the C is known that annexin II with and The of the is to the plasma membrane and is known to the Ca2+-binding sites and the binding A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google Scholar). The of the protein is to the and contains both the and C-terminal of the is that the terminus with p11 to AIIt, and the that the C terminus also the in to interact with the actin cytoskeleton the AIIt is its role as a the C-terminal domain of annexin II to be in the to bind to and the actin cytoskeleton. Annexin II tetramer (AIIt) is a multifunctional protein that in a with anionic phospholipids, F-actin, and Cell PubMed Scopus Google Scholar). to its ability to bind to actin and phospholipids, is to cells as a protein V. 1997; PubMed Scopus Google Scholar). is that the annexin II subunit of the protein the binding sites for the as as the sites for Cell PubMed Scopus Google Scholar). the of the F-actin-binding sites the protein The in the proteins and AIIt, and the of the F-actin binding domain the C terminus of the to that the C-terminal region of the annexin II subunit of AIIt be involved in F-actin binding. is known that the terminus of annexin II is for binding of p11 L. J. Cell Biol. PubMed Scopus Google Scholar, Sci. S. A. PubMed Scopus Google Scholar, M. T. J. Biol. Chem. Full Text PDF PubMed Google Scholar), a role to the C-terminal region of the we have site-directed mutagenesis to the C terminus of annexin II to its in F-actin binding. that of the amino acid of the C terminus of the annexin II subunit of AIIt the F-actin bundling activity of the protein by This to that the C terminus was involved in the interaction with F-actin. the F-actin binding activity of the annexin II of the F-actin binding of C-terminal truncations of annexin II that of or as as 9 amino acid also the F-actin binding activity of the the truncations in the C terminus of annexin II the interaction of annexin II with or heparin. The annexin II mutant proteins to and in a with a and as annexin mutant annexin II to a in a as annexin II to the annexin II to annexin II that was with we the ability of the AIIt, composed of wild-type p11 subunits and annexin II subunits to bundle F-actin AIIt composed of wild-type p11 subunits and annexin II subunits was unable to bundle F-actin. that the loss in F-actin bundling was to a in the binding of the mutant AIIt to F-actin. results for the first time that the C-terminal of the annexin II subunit of AIIt, LLYLCGGDD, contains F-actin binding domain of The of the F-actin binding domain to the C-terminal 9 amino acid of annexin II of the F-actin binding to also contains a actin-binding In a region the first amino acid of the protein the actin-binding site J. C. Res. 1996; PubMed Scopus Google Scholar, M. D. M. J. C. J. 1996; PubMed Scopus Google Scholar). is a with a for F-actin D. J. J. D. J. Biol. Chem. 1996; Full Text Full Text PDF PubMed Scopus Google Scholar, M. D. Res. 1999; PubMed Scopus Google Scholar, Curr. Opin. Cell Biol. PubMed Scopus Google Scholar). F-actin binding are in with the F-actin-binding sites of the proteins to amino acids D.J. Hall A. J. Cell Biol. 1997; PubMed Scopus Google Scholar, O. T. A. J. Cell Biol. 1994; PubMed Scopus Google Scholar). F-actin binding domain in amino acid of the protein P.J. Stull J.T. Cell 1997; PubMed Scopus Google Scholar). in light of the F-actin-binding sites of the the F-actin-binding site of is amino acid in M. P. M. G. J. Cell Biol. 1994; PubMed Scopus Google Scholar). In addition, the F-actin-binding sites the D. protein in to amino acid in the acid domain binding to F-actin S. M. 1999; PubMed Scopus Google Scholar). the of the F-actin-binding site of annexin II is with known for F-actin binding site to be the of F-actin-binding sites are the C terminus of annexin is known that the of F-actin-binding sites of T.D. Almo S. Quirk S. Vinson V. Lattman E.E. Annu. Rev. Cell Biol. 1994; 10: 207-249Crossref PubMed Scopus (86) Google Scholar). Interestingly, the region of annexin II that we contains the F-actin-binding site known to be of A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google Scholar). that a to the C-terminal amino acid of annexin II the binding of annexin II or AIIt to F-actin. we that the to the C-terminal amino acid of annexin II was unable to F-actin binding by annexin II or AIIt the that was to the C-terminal region of annexin was that was in the as the C-terminal region of annexin of a portion of with The inability of a to the C-terminal amino acids of annexin II to directly bind to F-actin two is that the C-terminal 9 amino acid of annexin II be of the F-actin-binding site and amino acids residues, by of annexin participate in of the the C-terminal region of annexin II F-actin, is that the C terminus interaction with amino acids to a that C-terminal amino acid to bind F-actin. is to that the was unable to the the of amino acid of annexin II to its was also that the C-terminal truncations of annexin II the F-actin binding activity of AIIt with the annexin This was is AIIt and annexin II that to the F-actin cytoskeleton. the binding of the p11 subunit to annexin II the C-terminal region of annexin II in a that the 9 amino acid to the F-actin-binding In is that the for amino acids to the interaction of the 9 C-terminal amino acid with F-actin is by the binding of p11 to annexin The is with of the F-actin-binding site of annexin II to the C is known that annexin II with and The of the is to the plasma membrane and is known to the Ca2+-binding sites and the binding A. S. J. A. P. V. C. J. J. Biol. 1996; PubMed Scopus Google Scholar). The of the protein is to the and contains both the and C-terminal of the is that the terminus with p11 to AIIt, and the that the C terminus also the in to interact with the actin cytoskeleton the AIIt is its role as a the C-terminal domain of annexin II to be in the to bind to and the actin cytoskeleton. G. and for and of the

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