Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms: Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding

Journal of Biological Chemistry

Volumn 277, Issue 47, 2002, Pages 45276-45284

  Zhang, Xiaohui ^a   Gan, Lixia ^a   Pan, Haiyun ^a   Guo, Shaodong ^a,f   He, Xiaowei ^a   Olson, Steven T ^b   Mesecar, Andrew ^c   Adam, Stephen ^d   Untermant, Terry G ^a,e,g  

^a UNIVERSITY OF ILLINOIS   (United States)

^b Department of Oral Medicine and Diagnostic Sciences   (United States)

^c UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^d NORTHWESTERN UNIVERSITY   (United States)

^e Vet Aff Chicago Hlth Care Syst   (United States)

^f HARVARD MEDICAL SCHOOL   (United States)

^g VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; DNA; GENES; PHOSPHORS; PROTEINS;

PHOSPHORYLATION;

BIOCHEMISTRY;

ALANINE; CELL DNA; HYBRID PROTEIN; PROTEIN KINASE B; SERINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FORKHEAD; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANISOTROPY; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELL NUCLEUS; CONTROLLED STUDY; DNA BINDING; EMBRYO; FLUORESCENCE; HUMAN; HUMAN CELL; INTRACELLULAR TRANSPORT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; PROTEIN TRANSPORT; REPORTER GENE; SIGNAL TRANSDUCTION; TRANSACTIVATION;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID MOTIFS; CELL LINE; CIRCULAR DICHROISM; DNA-BINDING PROTEINS; FORKHEAD TRANSCRIPTION FACTORS; GENES, REPORTER; GREEN FLUORESCENT PROTEINS; HUMANS; LUMINESCENT PROTEINS; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SERINE; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS;

AVES; BOS TAURUS; TRITICUM AESTIVUM;

EID: 0037160050     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M208063200     Document Type: Article

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