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Elucidation of protein interactions necessary for the maintenance of the BCR-ABL signaling complex

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00533597" target="_blank" >RIV/61388963:_____/20:00533597 - isvavai.cz</a>

  • Alternative codes found

    RIV/67985904:_____/20:00533597 RIV/00216224:14110/20:00116512 RIV/65269705:_____/20:00073337 RIV/00159816:_____/20:00073337

  • Result on the web

    <a href="https://asep.lib.cas.cz/arl-cav/cs/csg/?repo=crepo1&key=40768217680" target="_blank" >https://asep.lib.cas.cz/arl-cav/cs/csg/?repo=crepo1&key=40768217680</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00018-019-03397-7" target="_blank" >10.1007/s00018-019-03397-7</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Elucidation of protein interactions necessary for the maintenance of the BCR-ABL signaling complex

  • Original language description

    Many patients with chronic myeloid leukemia in deep remission experience return of clinical disease after withdrawal of tyrosine kinase inhibitors (TKIs). This suggests signaling of inactive BCR-ABL, which allows the survival of cancer cells, and relapse. We show that TKI treatment inhibits catalytic activity of BCR-ABL, but does not dissolve BCR-ABL core signaling complex, consisting of CRKL, SHC1, GRB2, SOS1, cCBL, p85a-PI3K, STS1 and SHIP2. Peptide microarray and co-immunoprecipitation results demonstrate that CRKL binds to proline-rich regions located in C-terminal, intrinsically disordered region of BCR-ABL, that SHC1 requires pleckstrin homology, src homology and tyrosine kinase domains of BCR-ABL for binding, and that BCR-ABL sequence motif located in disordered region around phosphorylated tyrosine 177 mediates binding of three core complex members, i.e., GRB2, SOS1, and cCBL. Further, SHIP2 binds to the src homology and tyrosine kinase domains of BCR-ABL and its inositol phosphatase activity contributes to BCR-ABL-mediated phosphorylation of SHC1. Together, this study characterizes protein-protein interactions within the BCR-ABL core complex and determines the contribution of particular BCR-ABL domains to downstream signaling. Understanding the structure and dynamics of BCR-ABL interactome is critical for the development of drugs targeting integrity of the BCR-ABL core complex.

  • 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

    10605 - Developmental biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cellular and Molecular Life Sciences

  • ISSN

    1420-682X

  • e-ISSN

  • Volume of the periodical

    77

  • Issue of the periodical within the volume

    19

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    19

  • Pages from-to

    3885-3903

  • UT code for WoS article

    000566036300001

  • EID of the result in the Scopus database

    2-s2.0-85076367083