The tumour-suppressor function of PTEN requires an N-terminal lipid-binding motif

Biochemical Journal

Volumn 379, Issue 2, 2004, Pages 301-307

  Walker, Steven M ^a,b   Leslie, Nick R ^a   Perera, Nevin M ^a   Batty, Ian H ^a   Downes, C Peter ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b BEATSON INSTITUTE FOR CANCER RESEARCH   (United Kingdom)

Author keywords

Lipid signalling; Phosphatase; Phosphoinositide

Indexed keywords

ASSAYS; CATALYSIS; CHROMOSOMES; ENZYMES; LIPIDS; MEMBRANES; MUTAGENESIS; PLASMAS; PROTEINS;

CELL PROFILERATION; CELLULAR ACTIVITY; MEMBRANE ORIENTATION; TUMOUR-SUPPRESSOR;

TUMORS;

ANION; LIPID; LIPID BINDING PROTEIN; PHOSPHATASE; PROTEIN; PROTEIN K13E; PROTEIN KINASE B; TENSIN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CATALYST; CELL LINE; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ASSAY; GENE MUTATION; HUMAN; LIPID SOLUBILITY; MYRISTYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; WILD TYPE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CELL MEMBRANE; LIPID METABOLISM; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHORIC MONOESTER HYDROLASES; POINT MUTATION; PTEN PHOSPHOHYDROLASE; SEQUENCE ALIGNMENT; TUMOR SUPPRESSOR PROTEINS;

EID: 2342631914     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031839     Document Type: Article

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