Publication Date:
1994-10-07
Description:
Members of a family of highly conserved proteins, termed 14-3-3 proteins, were found by several experimental approaches to associate with Raf-1, a central component of a key signal transduction pathway. Optimal complex formation required the amino-terminal regulatory domain of Raf-1. The association of 14-3-3 proteins and Raf-1 was not substantially affected by the activation state of Raf.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, H -- Xia, K -- Pallas, D C -- Cui, C -- Conroy, K -- Narsimhan, R P -- Mamon, H -- Collier, R J -- Roberts, T M -- AI22021/AI/NIAID NIH HHS/ -- CA57327/CA/NCI NIH HHS/ -- HD24926/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939632" target="_blank"〉PubMed〈/a〉
Keywords:
14-3-3 Proteins
;
3T3 Cells
;
Animals
;
Binding Sites
;
Cell Line
;
Enzyme Activation
;
Humans
;
Mice
;
Nerve Tissue Proteins/metabolism
;
Phosphorylation
;
Poly(ADP-ribose) Polymerases/metabolism
;
Protein-Serine-Threonine Kinases/*metabolism
;
Proteins/chemistry/*metabolism
;
Proto-Oncogene Proteins/*metabolism
;
Proto-Oncogene Proteins c-raf
;
*Signal Transduction
;
Spodoptera
;
*Tyrosine 3-Monooxygenase
;
Zinc Fingers
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
