PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly - Wikidata - awgldk - TriplyDB

PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly

PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly

http://www.wikidata.org/entity/Q34697985

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Post-translational modification-regulated leukocyte adhesion and migration The heavy chain has its day: regulation of myosin-II assembly Nonmuscle myosin-2: mix and match Pak1 regulates the orientation of apical polarization and lumen formation by distinct pathways Non-muscle myosin II regulates neuronal actin dynamics by interacting with guanine nucleotide exchange factors Non-muscle myosin II takes centre stage in cell adhesion and migration Dlc1 interaction with non-muscle myosin heavy chain II-A (Myh9) and Rac1 activation Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers.A regulatory motif in nonmuscle myosin II-B regulates its role in migratory front-back polarity The tumor suppressor Lgl1 regulates NMII-A cellular distribution and focal adhesion morphology to optimize cell migration.Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB Myosin IIB and F-actin control apical vacuolar morphology and histamine-induced trafficking of H-K-ATPase-containing tubulovesicles in gastric parietal cells.Life without double-headed non-muscle myosin II motor proteins.A proteomic study of myosin II motor proteins during tumor cell migration PRKC-ζ Expression Promotes the Aggressive Phenotype of Human Prostate Cancer Cells and Is a Novel Target for Therapeutic Intervention.Rac1-dependent phosphorylation and focal adhesion recruitment of myosin IIA regulates migration and mechanosensing.Oxidized LDL induces phosphorylation of non-muscle myosin IIA heavy chain in macrophages Loss of cell adhesion causes hydrocephalus in nonmuscle myosin II-B-ablated and mutated mice p21-activated kinase improves cardiac contractility during ischemia-reperfusion concomitant with changes in troponin-T and myosin light chain 2 phosphorylation Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells.TRPM7 regulates myosin IIA filament stability and protein localization by heavy chain phosphorylation.The phosphorylation of myosin II at the Ser1 and Ser2 is critical for normal platelet-derived growth factor induced reorganization of myosin filaments.p21-Activated kinase-1 and its role in integrated regulation of cardiac contractility.Various Themes of Myosin Regulation.p120 Catenin is required for normal tubulogenesis but not epithelial integrity in developing mouse pancreas.Protein kinase C zeta. A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins.Roles of P21-activated kinases and associated proteins in epithelial wound healing.Control of tumourigenesis by the Scribble/Dlg/Lgl polarity module.Mechanobiology of bone marrow stem cells: from myosin-II forces to compliance of matrix and nucleus in cell forms and fates.Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer.A small part of myosin IIB takes on a big role in cell polarity.Myosin IIA Heavy Chain Phosphorylation Mediates Adhesion Maturation and Protrusion in Three Dimensions.Conventional myosins - unconventional functions.aPKCζ affects directed cell migration through the regulation of myosin light chain phosphorylation.High resolution characterization of myosin IIC protein tailpiece and its effect on filament assembly.The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly.Myosin II tailpiece determines its paracrystal structure, filament assembly properties, and cellular localization.Filament-dependent and -independent localization modes of Drosophila non-muscle myosin II.The tumor suppressor Lgl1 regulates front-rear polarity of migrating cells.Myosin IIB deficiency in embryonic fibroblasts affects regulators and core members of the par polarity complex.

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P2860

PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly

http://www.wikidata.org/entity/Q34697985

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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prefLabel

PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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MBC.E05-11-1001

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Molecular Biology of the Cell

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PAK1 and aPKCzeta regulate myo ...... y regulating filament assembly

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Liron Even-Faitelson

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Shoshana Ravid

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P2860

Differential localization of myosin-II isozymes in human cultured cells and blood cells

A millennial myosin census

High-efficiency transformation of mammalian cells by plasmid DNA

Signaling through scaffold, anchoring, and adaptor proteins

Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity

The p21Rac/Cdc42-activated kinases (PAKs).

Protein kinase C autophosphorylates by an intrapeptide reaction.

Use of mass spectrometry to study signaling pathways.

New insights into the regulation of protein kinase C and novel phorbol ester receptors.

Implication of atypical protein kinase C isozymes lambda and zeta in Ras mediated reorganization of the actin cytoskeleton and cyclin D1-induction.

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10.1091/MBC.E05-11-1001

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7

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16611744

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phosphorylation

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1483025

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