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Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain.

Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Research Abstract Details 

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  • Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Abstract Text:

    Doublecortin-like kinase (DCLK) is widely expressed in postmitotic neurons throughout the embryonic nervous system. DCLK consists of an N-terminal doublecortin domain, responsible for its localization to microtubules, and a C-terminal serine-threonine kinase domain. Here we report that DCLK is a physiological substrate for the cysteine protease calpain. Cleavage of DCLK by calpain severs the kinase domain from its microtubule anchorage domain and releases it into the cytoplasm. The isolated kinase domain retains catalytic activity and is structurally similar to CPG16, a second product of the DCLK gene expressed in the adult brain that lacks the doublecortin domain. We propose that in neurons cleavage of DCLK by calpain represents a calcium responsive mechanism to regulate localization of the DCLK kinase domain.

    Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Publishing Authors By Initials

    For similar investigative techniques: genetic techniques: gene transfer techniques: transfection research abstracts see: investigative techniques: genetic techniques: gene transfer techniques: transfection research

    PUBMED ID PMID:

    MEDLINE DATE:

    Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: The Journal of biological chemistry

    VOLUME: 276

    Page Numbers: 36397-403

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 25

    MONTH: 07

    YEAR: 2001

    Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985121

    Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Keywords Mesh Terms:

    KEYWORDS: Transfection

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain. Information

    Substance Name: Calpain

    Registry Number: EC 3.4.22.-

    Grant and Affiliation Information for Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain.

    AFFILIATION: Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Biol Chem

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    Cleavage of doublecortin-like kinase by calpain releases an active kinase fragment from a microtubule anchorage domain Related Publications

     

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