Physical and Functional Interaction of Rabphilin-11 with Mammalian Sec13 Protein

Rab11a small G protein (Rab11p) is implicated in vesicle trafficking, especially vesicle recycling. We have previously isolated a downstream effector of Rab11p, named rabphilin-11. We found here that rabphilin-11 directly bound the mammalian counterpart of yeast Sec13 protein (mSec13p) in cell-free and intact cell systems. Yeast Sec13p is involved as a component of coat proteins II in the Sar1p-induced vesicle formation from the endoplasmic reticulum, but the precise role of mSec13p is unknown. The interaction of rabphilin-11 with mSec13p was enhanced by GTP-Rab11p. Rabphilin-11 localized on the vesicles in perinuclear regions and along microtubules oriented toward the plasma membrane, whereas mSec13p partly colocalized with rabphilin-11 in the perinuclear regions, most presumably the Golgi complex. Disruption of the rabphilin-11-mSec13p interaction by overexpression of the mSec13p-binding region of rabphilin-11 impaired vesicle trafficking. These results indicate that the rabphilin-11-mSec13p interaction is implicated in vesicle trafficking. Rab11a small G protein (Rab11p) is implicated in vesicle trafficking, especially vesicle recycling. We have previously isolated a downstream effector of Rab11p, named rabphilin-11. We found here that rabphilin-11 directly bound the mammalian counterpart of yeast Sec13 protein (mSec13p) in cell-free and intact cell systems. Yeast Sec13p is involved as a component of coat proteins II in the Sar1p-induced vesicle formation from the endoplasmic reticulum, but the precise role of mSec13p is unknown. The interaction of rabphilin-11 with mSec13p was enhanced by GTP-Rab11p. Rabphilin-11 localized on the vesicles in perinuclear regions and along microtubules oriented toward the plasma membrane, whereas mSec13p partly colocalized with rabphilin-11 in the perinuclear regions, most presumably the Golgi complex. Disruption of the rabphilin-11-mSec13p interaction by overexpression of the mSec13p-binding region of rabphilin-11 impaired vesicle trafficking. These results indicate that the rabphilin-11-mSec13p interaction is implicated in vesicle trafficking. amino acids coat proteins II endoplasmic reticulum maltose-binding protein polyacrylamide gel electrophoresis baby hamster kidney vesicular somatitis virus glycoprotein green fluorescent protein mammalian Sec13 protein Rab11p is a Rab small G protein family member that localizes to early endosomes, recycling endosomes, the trans-Golgi network membranes, and the post-Golgi secretory vesicles and regulates vesicle trafficking, especially vesicle recycling (1.Ohmori T. Takeyama Y. Ueda T. Hiroyoshi M. Nakanishi H. Ohyanagi H. Saitoh Y. Takai Y. Biochem. Biophys. Res. Commun. 1990; 169: 816-823Crossref PubMed Scopus (10) Google Scholar, 2.Chavrier P. Vingron M. Sander C. Simons K. Zerial M. Mol. Cell. Biol. 1990; 10: 6578-6585Crossref PubMed Scopus (178) Google Scholar, 3.Sakurada K. Uchida K. Yamaguchi K. Aisaka K. Ito S. Ohmori T. Takeyama Y. Ueda T. Hori Y. Ohyanagi H. Saitoh Y. Kaibuchi K. Takai Y. Biochem. Biophys. Res. Commun. 1991; 177: 1224-1232Crossref PubMed Scopus (28) Google Scholar, 4.Urbé S. Huber L.A. Zerial M. Tooze S.A. Parton R.G. FEBS Lett. 1993; 334: 175-182Crossref PubMed Scopus (186) Google Scholar, 5.Ullrich O. Reinsch S. Urbé S. Zerial M. Parton R.G. J. Cell Biol. 1996; 135: 913-924Crossref PubMed Scopus (1084) Google Scholar, 6.Chen W. Feng Y. Chen D. Wandinger-Ness A. Mol. Biol. Cell. 1998; 9: 3241-3257Crossref PubMed Scopus (320) Google Scholar, 7.Ren M. Xu G. Zeng J. Lemos-Chiarandini C.D. Adesnik M. Sabatini D.D. Proc. Natl. Acad. Sci. U. S. A. 1998; 95: 6187-6192Crossref PubMed Scopus (396) Google Scholar). Zeng et al. (8.Zeng J. Ren M. Gravotta D. Lemos-Chiarandini C.D. Lui M. Erdjument-Bromage H. Tempst P. Xu G. Shen T.H. Morimoto T. Adesnik M. Sabatini D.D. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 2840-2845Crossref PubMed Scopus (70) Google Scholar) and we (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar) have independently isolated the same downstream effector of Rab11p from bovine and rat, named Rab11BP and rabphilin-11, respectively. Rab11BP/rabphilin-11 (rabphilin-11) consists of 908 aa1 and contains one proline-rich region and six WD-40 repeats in addition to a Rab11p-binding domain. Free rabphilin-11 localizes in the cytosol, but upon binding to GTP-Rab11p, rabphilin-11 localizes to early endosomes, recycling endosomes, and the Golgi complex, as well as along microtubules oriented toward lamellipodia (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar), suggesting that GTP-Rab11p recruits rabphilin-11 to these membranes and exerts its function through rabphilin-11. However, the mode of action of the Rab11p-rabphilin-11 system in vesicle trafficking remains to be clarified. We searched here for a rabphilin-11-interacting molecule(s) by the yeast two-hybrid method and identified it as a mammalian counterpart of the yeast Sec13 protein (Sec13p). Yeast Sec13p is involved as a component of the COPII of the vesicles that bud from the ER in a Sar1p-dependent manner (10.Pryer N.K. Salama N.R. Schekman R. Kaiser C.A. J. Cell Biol. 1993; 120: 865-875Crossref PubMed Scopus (120) Google Scholar, 11.Salama N.R. Yeung T. Schekman R. EMBO J. 1993; 12: 4073-4082Crossref PubMed Scopus (176) Google Scholar, 12.Barlowe C. Orci L. Yeung T. Hosobuchi M. Hamamoto S. Salama N.R. Rexach M.F. Ravazzola M. Amherdt M. Schekman R. Cell. 1994; 77: 895-907Abstract Full Text PDF PubMed Scopus (1058) Google Scholar). When GDP-Sar1p is converted to GTP-Sar1p by the action of Sec12p, a GDP/GTP exchange protein of Sar1p (13.Nakano A. Brada D. Schekman R. J. Cell Biol. 1988; 107: 851-863Crossref PubMed Scopus (211) Google Scholar, 14.d'Enfert C. Barlowe C. Nishikawa S. Nakano A. Schekman R. Mol. Cell. Biol. 1991; 11: 5727-5734Crossref PubMed Scopus (63) Google Scholar, 15.Barlowe C. Schekman R. Nature. 1993; 365: 347-349Crossref PubMed Scopus (368) Google Scholar), Sec23 and Sec24p are recruited to the membrane of the ER followed by recruitment of Sec13p and Sec31p, causing bud formation (12.Barlowe C. Orci L. Yeung T. Hosobuchi M. Hamamoto S. Salama N.R. Rexach M.F. Ravazzola M. Amherdt M. Schekman R. Cell. 1994; 77: 895-907Abstract Full Text PDF PubMed Scopus (1058) Google Scholar, 16.Kuehn M.J. Herrmann J.M. Schekman R. Nature. 1998; 391: 187-190Crossref PubMed Scopus (328) Google Scholar, 17.Matsuoka K. Orci L. Amherdt M. Bednarek S.Y. Hamamoto S. Schekman R. Yeung T. Cell. 1998; 93: 263-275Abstract Full Text Full Text PDF PubMed Scopus (502) Google Scholar). When GTP-Sar1p is converted to GDP-Sar1p by the action of Sec23p, a GTPase-activating protein of Sar1p (18.Yoshihisa T. Barlowe C. Schekman R. Science. 1993; 259: 1466-1468Crossref PubMed Scopus (290) Google Scholar), the coated vesicles are uncoated (12.Barlowe C. Orci L. Yeung T. Hosobuchi M. Hamamoto S. Salama N.R. Rexach M.F. Ravazzola M. Amherdt M. Schekman R. Cell. 1994; 77: 895-907Abstract Full Text PDF PubMed Scopus (1058) Google Scholar, 17.Matsuoka K. Orci L. Amherdt M. Bednarek S.Y. Hamamoto S. Schekman R. Yeung T. Cell. 1998; 93: 263-275Abstract Full Text Full Text PDF PubMed Scopus (502) Google Scholar, 18.Yoshihisa T. Barlowe C. Schekman R. Science. 1993; 259: 1466-1468Crossref PubMed Scopus (290) Google Scholar). The mammalian counterpart of yeast Sec13p (mSec13p) has been isolated (19.Tang B.L. Peter F. Krijnse-Locker J. Low S.H. Griffiths G. Hong W. Mol. Cell. Biol. 1997; 17: 256-266Crossref PubMed Scopus (101) Google Scholar), but its precise role or mode of action remains unknown. We describe here the rabphilin-11-mSec13p interaction and its role in vesicle trafficking. Yeast transformations were performed by the lithium acetate method (20.Gietz D. St. Jean A. Woods R.A. Schiestl R.H. Nucleic Acids Res. 1992; 20: 1425Crossref PubMed Scopus (2899) Google Scholar). Yeast transformants were selected in dextrose-containing selection (SD) medium (21.Kamei T. Tanaka K. Hihara T. Umikawa M. Imamura H. Kikyo M. Ozaki K. Takai Y. J. Biol. Chem. 1998; 273: 28341-28345Abstract Full Text Full Text PDF PubMed Scopus (131) Google Scholar). The yeast reporter strain L40 expressing pLexA-rabphilin-11-1 (1–631 aa) was transformed with a human T cell cDNA library (MATCHMAKER human T cell oligo(dT)-primed library in pACT, CLONTECH). About 1.0 × 106 transformants were screened, and library plasmids from 16 positive clones were analyzed by transformation tests and DNA sequencing (22.Guarente L. Methods Enzymol. 1983; 101: 181-191Crossref PubMed Scopus (874) Google Scholar, 23.Vojtek A.B. Hollenberg S.M. Cooper J.A. Cell. 1993; 74: 205-214Abstract Full Text PDF PubMed Scopus (1663) Google Scholar). β-Galactosidase activity was measured by liquid and filter assays (23.Vojtek A.B. Hollenberg S.M. Cooper J.A. Cell. 1993; 74: 205-214Abstract Full Text PDF PubMed Scopus (1663) Google Scholar, 24.Miller J.H. Experiments in Molecular Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY1972Google Scholar). Where indicated, cotransformation was performed into yeast strain TAT7. Standard molecular biological techniques were used for construction of plasmids, DNA sequencing, and polymerase chain reaction (25.Sambrook J. Fritsch E.F. Maniatis T. Molecular Cloning : A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY1989Google Scholar). The cDNA fragments encoding several rabphilin-11 deletion mutants were inserted into pBTM116, encoding the DNA-binding domain of LexA: pLexA-rabphilin-11-1 (1–631 aa), -2 (300–631 aa), -3 (504–631 aa), -4 (632–908 aa), -5 (300–504 aa), -6 (607–730 aa), and -full (1–908 aa). The cDNA fragments encoding several mSec13p deletion mutants were inserted into pGAD424, encoding transcriptional activation domain of GAL4. The cDNA fragments encoding a dominant active mutant of Rab11p (Rab11pQ70LΔC, 1–211 aa) and a dominant negative mutant of Rab11p (Rab11pT25NΔC, 1–211 aa) were inserted into pGAD424. These Rab11ps did not possess the C-terminal lipid modification site to prevent association of Rab11p with the membranes (21.Kamei T. Tanaka K. Hihara T. Umikawa M. Imamura H. Kikyo M. Ozaki K. Takai Y. J. Biol. Chem. 1998; 273: 28341-28345Abstract Full Text Full Text PDF PubMed Scopus (131) Google Scholar). The cDNA fragment of full-length mSec13p was inserted into pMALC2 (New England BioLabs, Inc., Beverly, MA) and pGEX-4T-1 (Amersham Pharmacia Biotech) vectors. Mammalian expression plasmids were constructed by inserting full-length mSec13p and various truncated fragments of rabphilin-11 into pCIneo (Promega Corp., Madison, WI). Rabphilin-11-full and rabphilin-11-1 (1–631 aa) werein vitro translated using the TNT T7-coupled reticulocyte lysate system (Promega Corp.) and incubated with MBP or MBP-tagged mSec13p (100 pmol) prebound to an amylose resin column in buffer A (20 mm Tris/HCl, pH 7.5, 1 mm EDTA, 1 mm dithiothreitol, 1% Nonidet P-40, and 150 mmNaCl) at 4 °C for 90 min. After the beads were washed four times with the same buffer, the bound proteins were eluted by adding 100 μl of buffer A containing 10 mm maltose. The eluates were subjected to SDS-PAGE followed by autoradiography. The mouse brain cytosol was subjected to immunoprecipitation with 10 pmol of the anti-mSec13p antibody or the preimmune rabbit polyclonal antibody bound to 20 μl of protein A-Sepharose beads (Amersham Pharmacia Biotech). Comparable amounts of the pellets were subjected to SDS-PAGE followed by immunoblotting with the anti-rabphilin-11 antibody. The antibodies used here were prepared as described below. HeLa cells and BHK cells were supplied by Dr. S. Orita (Discovery Research Laboratory, Shionogi & Co. Ltd., Osaka, Japan). Both HeLa cells and BHK cells were cultured at 37 °C with a humidified atmosphere of 5% CO2 and 95% air in Dulbecco's modified Eagle's medium containing 10% fetal calf serum (Life Technologies, Inc.), 100 units/ml of penicillin, and 100 μg/ml of streptomycin. These cells were transiently transfected with the plasmids encoding the indicated proteins by use of Superfect reagent (Qiagen). A rabbit polyclonal antibody against mSec13p was raised against glutathioneS-transferase-tagged mSec13p. The antiserum was affinity-purified with MBP-tagged mSec13p covalently coupled to CNBr-activated Sepharose beads (Amersham Pharmacia Biotech). An anti-rabphilin-11 antibody was obtained as described (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar). Hybridoma cells expressing the mouse monoclonal anti-Myc antibody (9E10) were purchased from American Type Culture Collection (Manassas, VA). An anti-Golgi p58 antibody was purchased from Sigma. An anti-Calnexin antibody was purchased from StressGenn Biotechnologies Corp. (Victoria, Canada). Second antibodies for immunofluorescence microscopy were obtained from Chemicon International, Inc. (Temecula, CA). Immunofluorescence staining was performed as described (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar). The cells were examined by use of an Eclipse E800 immunofluorescence microscope (Nikon, Tokyo, Japan). Equal amounts of the plasmids encoding several rabphilin-11 deletion mutants and GFP-tagged VSV G protein were used for cotransfection experiments. After 17 h, transfected BHK cells were incubated at 20 °C for 2 h. Parallel samples were transferred to 37 °C for 1 h immediately after incubation at 20 °C. Cells were then fixed and examined by immunofluorescence microscopy. We first attempted to isolate a rabphilin-11-interacting protein(s) by use of the yeast two-hybrid method with the N-terminal fragment (rabphilin-11-1, 1–631 aa) as a bait from a human T cell cDNA library. Screening of 1 × 106 transformants yielded 16 positive clones, and 6 of these clones encoded full-length mSec13p. One of the six clones was selected for further analysis. The selected clone (clone 5) indeed interacted with rabphilin-11-1 (Fig.1 A). This clone also interacted with full-length rabphilin-11 (rabphilin-11-full), to a lesser extent, but did not interact with the C-terminal fragment (rabphilin-11-4, 632–908 aa) (Fig. 1 A). To examine whether rabphilin-11 directly interacts with mSec13p, the binding of in vitro translated [35S]methionine-labeled rabphilin-11-1 (1–631 aa) or rabphilin-11-full to MBP-tagged recombinant mSec13p was examined. Both rabphilin-11-1 and rabphilin-11-full directly interacted with mSec13p (Fig. 1 B, a and b). The interaction of rabphilin-11 with mSec13p was confirmed by coimmunoprecipitation from the mouse brain cytosol (Fig. 1 C). Moreover, subcellular localization analysis in HeLa cells showed that overexpressed Myc-tagged mSec13p localized at the ER and the Golgi complex (Fig.2 , A and B), whereas endogenous rabphilin-11 localized in perinuclear regions and along microtubules oriented toward the plasma membrane; Myc-tagged mSec13p and rabphilin-11 colocalized in perinuclear regions, most presumably the Golgi complex (Fig. 2 C). Essentially equivalent results were obtained in BHK cells and Madin-Darby canine kidney cells (data not shown). These results suggest that rabphilin-11 directly interacts with mSec13p in both cell-free and intact cell systems. We next studied the mSec13p-binding region of rabphilin-11 by the yeast two-hybrid method. Rabphilin-11-full interacted with mSec13p to some extent, but the region (rabphilin-11-3, 504–631 aa) that contains the second and third WD-40 repeats and is located next to the Rab11p-binding region (300–504 aa), interacted with mSec13p to a greater extent (Fig. 3 A). Other regions, excluding this region, did not interact with mSec13p. These results suggest that a region(s) other than the mSec13p-binding region masks this region, thereby hindering the interaction with mSec13p, and that another factor is necessary to open this folded structure. We next examined the effect of Rab11p on the rabphilin-11-mSec13p interaction by the yeast two-hybrid method. The rabphilin-11-full-mSec13p interaction was greater upon coexpression with a dominant active mutant of Rab11p (Rab11pQ70LΔC) than upon coexpression with a dominant negative mutant of Rab11p (Rab11pT25NΔC) or with no expression of these mutants (Fig. 3 B), suggesting that the rabphilin-11-full-mSec13p interaction is enhanced by the binding of GTP-Rab11p to rabphilin-11. This enhancement, however, did not reach the level of the rabphilin-11-3-mSec13p interaction. We attempted to determine the rabphilin-11-binding region of mSec13p by the same method. The N-terminal one-third (1–187 aa), the middle one-third (135–249 aa), or the C-terminal one-third (249–323 aa) of mSec13p did not interact with rabphilin-11-2 (300–631 aa) (data not shown), suggesting that the whole structure of mSec13p is necessary for the interaction with rabphilin-11. Finally, we examined whether the rabphilin-11-mSec13p interaction is important in vesicle trafficking. For this purpose, we took advantage of the VSV G protein transport system. VSV G protein is a membrane protein encoded by the vesicular somatitis virus (which is transported to the cell along the and be as an of vesicle trafficking W. Feng Y. Chen D. Wandinger-Ness A. Mol. Biol. Cell. 1998; 9: 3241-3257Crossref PubMed Scopus (320) Google Scholar, Wandinger-Ness A. H. Griffiths G. Simons K. M. of the Scholar, Laboratory Methods in and Scholar, K. J. Nature. 1997; PubMed Scopus Google Scholar). described W. Feng Y. Chen D. Wandinger-Ness A. Mol. Biol. Cell. 1998; 9: 3241-3257Crossref PubMed Scopus (320) Google Scholar), in BHK GFP-tagged VSV G protein in perinuclear regions, presumably to the Golgi complex, by incubation at 20 °C for 2 h and was transported to the plasma membrane by incubation at 37 °C for 1 h (Fig. 4 a of a Myc-tagged dominant negative mutant of Rab11p transport of G protein to the cell as with cells (data not shown), with W. Feng Y. Chen D. Wandinger-Ness A. Mol. Biol. Cell. 1998; 9: 3241-3257Crossref PubMed Scopus (320) Google Scholar). overexpression of the Rab11p-binding region of rabphilin-11 aa) or the mSec13p-binding region of rabphilin-11 504–631 aa) the transport of G protein (Fig. 4 B, a However, overexpression of Myc-tagged rabphilin-11-full (data not or Myc-tagged rabphilin-11-2 (300–631 aa), contains both the Rab11p-binding and mSec13p-binding regions, did not this transport (Fig. 4 These with the that Rab11p regulates membrane vesicle transport W. Feng Y. Chen D. Wandinger-Ness A. Mol. Biol. Cell. 1998; 9: 3241-3257Crossref PubMed Scopus (320) Google Scholar), suggest that the rabphilin-11-mSec13p interaction is important in vesicle We have here that rabphilin-11 directly interacts with mSec13p by use of yeast column and The interaction of full-length rabphilin-11 with mSec13p is than that of the mSec13p-binding region of rabphilin-11 with mSec13p, suggesting that a region(s) other than the mSec13p-binding region masks this region and the interaction with mSec13p. the binding of GTP-Rab11p to full-length rabphilin-11 its interaction with mSec13p, suggesting that the region be a region and that the binding of GTP-Rab11p to this region directly or the mSec13p-binding However, the by GTP-Rab11p not reach the level of interaction of the mSec13p-binding region of rabphilin-11 with mSec13p. has previously been that is some factor that the of the region of rabphilin-11 (8.Zeng J. Ren M. Gravotta D. Lemos-Chiarandini C.D. Lui M. Erdjument-Bromage H. Tempst P. Xu G. Shen T.H. Morimoto T. Adesnik M. Sabatini D.D. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 2840-2845Crossref PubMed Scopus (70) Google Scholar), suggesting that a region(s) other than the region also be involved in this and We have previously that rabphilin-11 is with membrane presumably in a manner (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar). The precise localization of mSec13p is not but by with yeast Sec13p (10.Pryer N.K. Salama N.R. Schekman R. Kaiser C.A. J. Cell Biol. 1993; 120: 865-875Crossref PubMed Scopus (120) Google Scholar, 11.Salama N.R. Yeung T. Schekman R. EMBO J. 1993; 12: 4073-4082Crossref PubMed Scopus (176) Google Scholar), mSec13p also on this is the one of the interaction on vesicles is that GTP-Rab11p first to rabphilin-11 to the structure to the association of the complex on the The of GTP-Rab11p also be involved in the association of the complex with the but the binding of the complex be by the interaction with mSec13p. has been that yeast Sec13p in the formation of of the vesicles that bud from the complex Kaiser C.A. J. Cell Biol. 1997; PubMed Scopus Google Scholar) and COPII coated vesicles that bud from the ER (10.Pryer N.K. Salama N.R. Schekman R. Kaiser C.A. J. Cell Biol. 1993; 120: 865-875Crossref PubMed Scopus (120) Google Scholar, 11.Salama N.R. Yeung T. Schekman R. EMBO J. 1993; 12: 4073-4082Crossref PubMed Scopus (176) Google Scholar, 12.Barlowe C. Orci L. Yeung T. Hosobuchi M. Hamamoto S. Salama N.R. Rexach M.F. Ravazzola M. Amherdt M. Schekman R. Cell. 1994; 77: 895-907Abstract Full Text PDF PubMed Scopus (1058) Google Scholar, 17.Matsuoka K. Orci L. Amherdt M. Bednarek S.Y. Hamamoto S. Schekman R. Yeung T. Cell. 1998; 93: 263-275Abstract Full Text Full Text PDF PubMed Scopus (502) Google Scholar). the Sec13p be involved in protein transport from the Golgi complex to the plasma membrane Kaiser C.A. J. Cell Biol. 1997; PubMed Scopus Google Scholar). We have here that mSec13p localizes in perinuclear regions, presumably the ER and the Golgi complex, the complex at the Golgi complex. addition to these the complex localizes to early endosomes, recycling endosomes, and secretory vesicles along microtubules oriented toward the plasma membrane (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar). These with (9.Mammoto A. Ohtsuka T. Hotta I. Sasaki T. Takai Y. J. Biol. Chem. 1999; 274: 25517-25524Abstract Full Text Full Text PDF PubMed Scopus (81) Google Scholar, Kaiser C.A. J. Cell Biol. 1997; PubMed Scopus Google Scholar), suggest that the rabphilin-11-mSec13p interaction regulates the transport of the vesicles from the Golgi complex to the microtubules oriented toward the plasma the vesicles on the mSec13p from the vesicles and be with yeast mSec13p also be involved in the at from the Golgi complex, and this be by small G proteins D. R.A. Proc. Natl. Acad. Sci. U. S. A. 1992; PubMed Scopus Google Scholar, Orci L. J. Biol. Chem. 1993; Full Text PDF PubMed Google Scholar, Cell. 1993; Full Text PDF PubMed Scopus Google Scholar, J.A. S. J. Cell Biol. 1993; PubMed Scopus Google Scholar). the coated vesicles are from the Golgi complex, are uncoated and transported to the plasma membrane along Rab family are involved in the of vesicles to the membranes C. Biochem. 1994; PubMed Scopus Google Scholar, Cell Biol. 1994; PubMed Scopus Google Scholar, Y. Sasaki T. H. Nakanishi H. 1996; PubMed Scopus Google Scholar, P. Zerial M. Cell Biol. 1997; 9: PubMed Scopus Google Scholar). Rab11p is also be involved in these the rabphilin-11-mSec13p interaction of small G and Rab are necessary for of the mode of action of the rabphilin-11-mSec13p interaction in vesicle trafficking. We Dr. of for the encoding G

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.