Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00478474" target="_blank" >RIV/61388963:_____/17:00478474 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/17:10363658
Result on the web
<a href="https://www.nature.com/articles/s41598-017-08303-4" target="_blank" >https://www.nature.com/articles/s41598-017-08303-4</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-017-08303-4" target="_blank" >10.1038/s41598-017-08303-4</a>
Alternative languages
Result language
angličtina
Original language name
Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners
Original language description
CAS is a docking protein downstream of the proto-oncogene Src with a role in invasion and metastasis of cancer cells. The CAS SH3 domain is indispensable for CAS-mediated signaling, but structural aspects of CAS SH3 ligand binding and regulation are not well understood. Here, we identified the consensus CAS SH3 binding motif and structurally characterized the CAS SH3 domain in complex with ligand. We revealed the requirement for an uncommon centrally localized lysine residue at position +2 of CAS SH3 ligands and two rather dissimilar optional anchoring residues, leucine and arginine, at position +5. We further expanded the knowledge of CAS SH3 ligand binding regulation by manipulating tyrosine 12 phosphorylation and confirmed the negative role of this phosphorylation on CAS SH3 ligand binding. Finally, by exploiting the newly identified binding requirements of the CAS SH3 domain, we predicted and experimentally verified two novel CAS SH3 binding partners, DOK7 and GLIS2.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
7
Issue of the periodical within the volume
Aug 14
Country of publishing house
GB - UNITED KINGDOM
Number of pages
18
Pages from-to
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UT code for WoS article
000407559800024
EID of the result in the Scopus database
2-s2.0-85027462937