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Neurabins recruit protein phosphatase-1 and inhibitor-2 to the actin cytoskeleton.

Authors: Terry-Lorenzo, RT  Elliot, E  Weiser, DC  Prickett, TD  Brautigan, DL  Shenolikar, S 
Citation: Terry-Lorenzo RT, etal., J Biol Chem 2002 Nov 29;277(48):46535-43. Epub 2002 Sep 21.
Pubmed: (View Article at PubMed) PMID:12270929
DOI: Full-text: DOI:10.1074/jbc.M206960200

Inhibitor-2 (I-2) bound protein phosphatase-1 (PP1) and several PP1-binding proteins from rat brain extracts, including the actin-binding proteins, neurabin I and neurabin II. Neurabins from rat brain lysates were sedimented by I-2 and its structural homologue, I-4. The central domain of both neurabins bound PP1 and I-2, and mutation of a conserved PP1-binding motif abolished neurabin binding to both proteins. Microcystin-LR, a PP1 inhibitor, also attenuated I-2 binding to neurabins. Immunoprecipitation of neurabin I established its association with PP1 and I-2 in HEK293T cells and suggested that PP1 mediated I-2 binding to neurabins. The C terminus of I-2, although not required for PP1 binding, facilitated PP1 recruitment by neurabins, which also targeted I-2 to polymerized F-actin. Mutations that attenuated PP1 binding to I-2 and neurabin I suggested distinct and overlapping sites for these two proteins on the PP1 catalytic subunit. Immunocytochemistry in epithelial cells and cultured hippocampal neurons showed that endogenous neurabin II and I-2 colocalized at actin-rich structures, consistent with the ability of neurabins to target the PP1.I-2 complex to actin cytoskeleton and regulate cell morphology.

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CRRD Object Information
CRRD ID: 1299366
Created: 2004-06-01
Species: All species
Last Modified: 2004-06-01
Status: ACTIVE



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