The phosphorylation status and anti-apoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria

FEBS Letters

Volumn 569, Issue 1-3, 2004, Pages 249-255

  Tamura, Yuki ^a,b   Simizu, Siro ^a   Osada, Hiroyuki ^a,b  

^a Japan Science and Technology Agency   (Japan)

^b SAITAMA UNIVERSITY   (Japan)

Author keywords

Apoptosis; Bcl 2; CPT, camptothecin; ERK, extracellular signal regulated kinase 1 and 2; Extracellular signal regulated kinase; JNK, c Jun N terminal kinase 1 and 2; MAPK, mitogen activated protein kinase; Phosphorylation; Protein phosphatase 2A

Indexed keywords

MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN BCL 2;

APOPTOSIS; ARTICLE; CELL LINE; DEPHOSPHORYLATION; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MITOCHONDRION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION;

APOPTOSIS; CARCINOMA, HEPATOCELLULAR; CELL LINE, TUMOR; ENZYME INHIBITORS; HELA CELLS; HUMANS; KINETICS; LIVER NEOPLASMS; MITOCHONDRIA; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASES; MUTAGENESIS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PLASMIDS; PROTO-ONCOGENE PROTEINS C-BCL-2; RECOMBINANT PROTEINS; SEQUENCE DELETION;

EID: 3042549655     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.06.003     Document Type: Article

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