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The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family.

The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Research Abstract Details 

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  • The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Abstract Text:

    cheng-gee kohCheng-Gee Koh,e-jean tanE-Jean Tan,edward manserEdward Manser,louis limLouis Lim,

    The Rho GTPases are involved in many signaling pathways and cellular functions, including the organization of the actin cytoskeleton, regulation of transcription, cell motility, and cell division. The p21 (Cdc42/Rac)-activated kinase PAK mediates a number of biological effects downstream of these Rho GTPases (reviewed by [1]). The phosphorylation state of mammalian PAK is highly regulated: upon binding of GTPases, PAK is potently activated by autophosphorylation at multiple sites, although the mechanisms of PAK downregulation are not known. We now report two PP2C-like serine/threonine phosphatases (POPX1 and POPX2) that efficiently inactivate PAK. POPX1 was isolated as a binding partner for the PAK interacting guanine nucleotide exchange factor PIX. The dephosphorylating activity of POPX correlates with an ability to block the in vivo effects of active PAK. Consonant with these effects on PAK, POPX can also inhibit actin stress fiber breakdown and morphological changes driven by active Cdc42(V12). The association of the POPX phosphatases with PAK complexes may allow PAK to cycle rapidly between active and inactive states; it represents a unique regulatory component of the signaling pathways of the PAK kinase family.

    The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Publishing Authors By Initials

    cg kohCG Koh,ej tanEJ Tan,e manserE Manser,l limL Lim,

    For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research

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    The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Current biology : CB

    VOLUME: 12

    Page Numbers: 317-21

    Journal Abbreviation: Curr. Biol.

    ISSN: 0960-9822

    DAY: 19

    MONTH: Feb

    YEAR: 2002

    The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9107782

    The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Keywords Mesh Terms:

    KEYWORDS: p21-Activated Kinases

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Information

    Substance Name: cdc42 GTP-Binding Protein

    Registry Number: EC 3.6.5.2

    Grant and Affiliation Information for The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family.

    AFFILIATION: Institute of Molecular and Cell Biology, 30 Medical Drive, 117609, Singapore, Singapore. mcbkohcg@imcb.nus.edu.sg

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: Curr Biol

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    The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family Related Publications

     

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