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Record W2104562394 · doi:10.1111/febs.12420

The unique N‐terminal region of <scp>SRMS</scp> regulates enzymatic activity and phosphorylation of its novel substrate docking protein 1

2013· article· en· W2104562394 on OpenAlexaff
Raghuveera Kumar Goel, Sayem Miah, Kristin A. Black, Natasha Kalra, Chenlu Dai, Kiven Erique Lukong

Bibliographic record

VenueFEBS Journal · 2013
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Kinase Regulation and GTPase Signaling
Canadian institutionsUniversity of Saskatchewan
Fundersnot available
KeywordsFYNProto-oncogene tyrosine-protein kinase SrcTyrosine kinaseSH3 domainKinaseBiologyBiochemistrySrc family kinaseTyrosine-protein kinase CSKCell biologyChemistrySignal transduction

Abstract

fetched live from OpenAlex

SRMS (Src‐related tyrosine kinase lacking C‐terminal regulatory tyrosine and N‐terminal myristoylation sites) belongs to a family of nonreceptor tyrosine kinases, which also includes breast tumour kinase and Fyn‐related kinase. SRMS , similar to breast tumour kinase and Fyn‐related kinase, harbours a Src homology 3 and Src homology 2, as well as a protein kinase domain. However, unlike breast tumour kinase and Fyn‐related kinase, SRMS lacks a C‐terminal regulatory tail but distinctively possesses an extended N‐terminal region. Both breast tumour kinase and Fyn‐related kinase play opposing roles in cell proliferation and signalling. SRMS , however, is an understudied member of this family. Although cloned in 1994, information on the biochemical, cellular and physiological roles of SRMS remains unreported. The present study is the first to explore the expression pattern of SRMS in breast cancers, its enzymatic activity and autoregulatory elements, and the characterization of docking protein 1 as its first bonafide substrate. We found that, similar to breast tumour kinase, SRMS is highly expressed in most breast cancers compared to normal mammary cell lines and tissues. We generated a series of SRMS point and deletion mutants and assessed enzymatic activity, subcellular localization and substrate recognition. We report for the first time that ectopically‐expressed SRMS is constitutively active and that its N‐terminal region regulates the enzymatic activity of the protein. Finally, we present evidence indicating that docking protein 1 is a direct substrate of SRMS . Our data demonstrate that, unlike members of the Src family, the enzymatic activity of SRMS is regulated by the intramolecular interactions involving the N‐terminus of the enzyme and that docking protein 1 is a bona fide substrate of SRMS . Structured digital abstract SRMS physically interacts with Dok-1 by pull down (View Interaction: 1 , 2 ) Dok-1 physically interacts with SRMS by anti bait coimmunoprecipitation (View Interaction: 1 , 2 , 3 ) SRMS phosphorylates Dok-1 by protein kinase assay ( View interaction ) Dok-1 physically interacts with SRMS by anti tag coimmunoprecipitation ( View interaction )

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.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.014
Threshold uncertainty score0.347

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.014
GPT teacher head0.235
Teacher spread0.220 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations25
Published2013
Admission routes1
Has abstractyes

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