Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein moesin

Journal of Biological Chemistry

Volumn 290, Issue 18, 2015, Pages 11384-11392

  Wei, Zhiyi ^a,b   Li, Youjun ^a   Ye, Fei ^a   Zhang, Mingjie ^a  

^a HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

^b SOUTHERN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CELL GROWTH; GROWTH KINETICS; PHOSPHORYLATION;

ACTIN-BINDING PROTEINS; CELL POLARITY; CYTOPLASMIC TAIL; GROWTH CONTROL; POLARITY ESTABLISHMENT; STRUCTURAL BASIS;

PROTEINS;

BINDING PROTEIN; CRUMB PROTEIN; MEMBRANE PROTEIN; MOESIN; MULTIPROTEIN COMPLEX; PDZ PROTEIN; PROTEIN 4.1 EZRIN RADIXIN MOESIN CRUMB CYTOPLASMIC TAIL COMPLEX; PROTEIN ASSOCIATED WITH LIN7 1; PROTEIN KINASE C; UNCLASSIFIED DRUG; ACTIN; ACTIN BINDING PROTEIN; CRUMBS PROTEIN, DROSOPHILA; CYTOSKELETON PROTEIN; DROSOPHILA PROTEIN; EZRIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; RADIXIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL GROWTH; CELL POLARITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASMIC TAIL; GROWTH INHIBITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CYTOPLASM; DROSOPHILA MELANOGASTER; ENZYME SPECIFICITY; HUMAN; METABOLISM; MOLECULAR GENETICS; MOUSE; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE;

ACTINS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL POLARITY; CYTOPLASM; CYTOSKELETAL PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; HUMANS; MEMBRANE PROTEINS; MICE; MICROFILAMENT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHORYLATION; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84929493795     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.643791     Document Type: Article

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