p116Rip targets myosin phosphatase to the actin cytoskeleton and is essential for RhoA/ROCK-regulated neuritogenesis

Molecular Biology of the Cell

Volumn 15, Issue 12, 2004, Pages 5516-5527

  Mulder, Jacqueline ^a   Ariaens, Aafke ^a   Van Den Boomen, Dick ^a   Moolenaar, Wouter H ^a  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; F ACTIN; LEUCINE ZIPPER PROTEIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN PHOSPHATASE; MYOSIN PHOSPHATASE; PHOSPHATASE; PROTEIN P116 RIP; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA RHO KINASE; UNCLASSIFIED DRUG; DETERGENT; M RIP PROTEIN, HUMAN; M-RIP PROTEIN, HUMAN; P116RIP PROTEIN, MOUSE; P116RIP PROTEIN, RAT; PROTEIN SERINE THREONINE KINASE; PROTEIN SUBUNIT; RHO-ASSOCIATED KINASE; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL SPREADING; CONTROLLED STUDY; CYTOSKELETON; ENZYME ACTIVATION; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME SUBUNIT; GROWTH CONE; HUMAN; HUMAN CELL; NERVE FIBER GROWTH; NERVOUS SYSTEM DEVELOPMENT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; REGULATORY MECHANISM; RNA INTERFERENCE; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CERCOPITHECUS; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; MOUSE; NEURITE; PHOSPHORYLATION; PROTEIN BINDING; RAT; SOLUBILITY;

ACTINS; ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CERCOPITHECUS AETHIOPS; CYTOSKELETON; DETERGENTS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MICE; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; MYOSIN-LIGHT-CHAIN PHOSPHATASE; NEURITES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN SUBUNITS; PROTEIN-SERINE-THREONINE KINASES; RATS; RHOA GTP-BINDING PROTEIN; RNA INTERFERENCE; SOLUBILITY;

EID: 9444261967     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-04-0275     Document Type: Article

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