Modulation of fatty acid synthase degradation by concerted action of p38 MAP kinase, E3 ligase COP1, and SH2-tyrosine phosphatase Shp2

Journal of Biological Chemistry

Volumn 288, Issue 6, 2013, Pages 3823-3830

  Yu, Jianxiu ^a,b   Deng, Rong ^a   Zhu, Helen H ^b   Zhang, Sharon S ^b   Zhu, Changhong ^a   Montminy, Marc ^c   Davis, Roger ^d   Feng, Gen Sheng ^b  

^a SHANGHAI JIAO TONG UNIVERSITY SCHOOL OF MEDICINE   (China)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^d UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX FORMATIONS; CYTOPLASMIC TYROSINE KINASE; E3 LIGASE; FATTY ACID SYNTHASE; IN-CONTROL; LIPID METABOLISMS; MAP KINASE; MOUSE LIVER; NOVEL FUNCTIONS; PROTEIN DEGRADATION; PROTEIN LEVEL; SIGNALING PATHWAYS; SRC-HOMOLOGY; TYROSINE PHOSPHATASE; UBIQUITINATION;

CYTOLOGY; METABOLISM; PHOSPHATASES; PHOSPHORYLATION; PHYSIOLOGY;

AMINO ACIDS;

ADAPTOR PROTEIN; FATTY ACID SYNTHASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN TYROSINE PHOSPHATASE SHP 2; STEROL REGULATORY ELEMENT BINDING PROTEIN 1C; UBIQUITIN PROTEIN LIGASE COP1;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CANCER INHIBITION; CELL ACTIVITY; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME DEGRADATION; ENZYME REGULATION; ENZYME STRUCTURE; FASN GENE; GENE; GENE EXPRESSION; HUMAN; HUMAN CELL; LIPID METABOLISM; MOLECULAR MECHANICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SYNTHESIS REGULATION; SIGNAL TRANSDUCTION; UBIQUITINATION;

3T3 CELLS; ANIMALS; FATTY ACID SYNTHETASE COMPLEX, TYPE I; HELA CELLS; HUMANS; LIPID METABOLISM; LIVER; MICE; MICE, KNOCKOUT; NUCLEAR PROTEINS; P38 MITOGEN-ACTIVATED PROTEIN KINASES; PANCREAS; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11; PROTEOLYSIS; UBIQUITIN-PROTEIN LIGASES;

EID: 84873643973     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.397885     Document Type: Article

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