A polarity complex of mPar-6 and atypical PKC binds, phosphorylates and regulates mammalian Lgl

Nature Cell Biology

Volumn 5, Issue 4, 2003, Pages 301-308

  Plant, Pamela J ^a   Fawcett, James P ^a   Lin, Dan C C ^a,b   Holdorf, Amy D ^a   Binns, Kathleen ^a,b   Kulkarni, Sarang ^a   Pawson, Tony ^a,b  

^a MOUNT SINAI HOSPITAL   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEIN KINASE C; PROTEIN LGL; PROTEIN PAR 6; SERINE; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL DIVISION; CELL LINE; CELL POLARITY; CONTROLLED STUDY; ENZYME SUBSTRATE; FIBROBLAST; GENETIC CONSERVATION; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; REGULATORY MECHANISM; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; CELL POLARITY; COS CELLS; DROSOPHILA PROTEINS; EUKARYOTIC CELLS; HUMANS; MACROMOLECULAR SUBSTANCES; MICE; MULTIPROTEIN COMPLEXES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEINS; TUMOR CELLS, CULTURED; TUMOR SUPPRESSOR PROTEINS; WOUND HEALING;

ANIMALIA; DROSOPHILA MELANOGASTER; MAMMALIA; MELANOGASTER; MURINAE;

EID: 0037385561     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb948     Document Type: Article

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