Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.
摘要：
The highly conserved and ubiquitously expressed 14-3-3 family of proteins bind to a variety of proteins involved in signal transduction and cell cycle regulation. The nature and specificity of 14-3-3 binding is, however, not known. Here we show that 14-3-3 is a specific phosphoserine-binding protein. Using a panel of phosphorylated peptides based on Raf-1, we have defined the 14-3-3 binding motif and show that most of the known 14-3-3 binding proteins contain the motif. Peptides containing the motif could disrupt 14-3-3 complexes and inhibit maturation of Xenopus laevis oocytes. These results suggest that the interactions of 14-3-3 with signaling proteins are critical for the activation of signaling proteins. Our findings also suggest novel roles for serine/threonine phosphorylation in the assembly of protein-protein complexes.
展开
DOI：
10.1016/S0092-8674(00)81067-3
被引量：
年份：
1996
Elsevier
Taylor & Francis
Elsevier
(全网免费下载)
Semantic Scholar
(全网免费下载)
万方医学
查看更多
dx.doi.org
NCBI
www.cell.com
NCBI
Europe PMC
Cell Press
(全网免费下载)
EureKaMag.com
(全网免费下载)
ResearchGate
EBSCO
jcs.biologists.org
mcponline.org
molbiolcell.org
embor.embopress.org
scienceopen.com
199.171.202.195
readcube.com
deepdyve.com
physiologyonline.physiology.org
mendeley.com
jacionline.org
core.ac.uk
(全网免费下载)
plantphysiol.org
Elsevier
(全网免费下载)
Semantic Scholar
(全网免费下载)
Cell Press
(全网免费下载)
EureKaMag.com
(全网免费下载)
core.ac.uk
(全网免费下载)
通过文献互助平台发起求助，成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
