共 33 条
I-proteins - a proposed switch in myotubularin function
被引:8
作者:

Clague, MJ
论文数: 0 引用数: 0
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机构: Univ Liverpool, Physiol Lab, Liverpool L69 3BX, Merseyside, England

Dove, SK
论文数: 0 引用数: 0
h-index: 0
机构: Univ Liverpool, Physiol Lab, Liverpool L69 3BX, Merseyside, England

Barr, FA
论文数: 0 引用数: 0
h-index: 0
机构: Univ Liverpool, Physiol Lab, Liverpool L69 3BX, Merseyside, England
机构:
[1] Univ Liverpool, Physiol Lab, Liverpool L69 3BX, Merseyside, England
[2] Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England
[3] Max Planck Inst Biochem, Dept Cell Biol, D-82152 Martinsried, Germany
基金:
英国惠康基金;
关键词:
D O I:
10.1016/j.tibs.2003.12.005
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
In this article, we consider the functions of the myotubularins - a large family of phosphoinositide 3-phosphatases. By analogy with the phosphatidylinositol 3-phosphatase PTEN (phosphatase and tensin homolog deleted in chromosome ten) and many protein phosphatases, it has been proposed that the primary function of this protein family is to regulate substrate levels, in this case phosphatidylinositol (3)-phosphate. We propose an alternate, or additional, function that is analogous to the G-protein family of phosphatases, which use nucleotide-dependent conformational changes to transduce signals or do mechanical work.
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页码:58 / 61
页数:4
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