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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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

  • UT code for WoS article

    000407559800024

  • EID of the result in the Scopus database

    2-s2.0-85027462937