Sphingosine Kinases: Emerging Structure-Function Insights

被引：61

作者：

Adams, David R. ^{[1
]}

Pyne, Susan ^{[2
]}

Pyne, Nigel J. ^{[2
]}

机构：

[1] Heriot Watt Univ, Inst Chem Sci, Edinburgh EH14 4AS, Midlothian, Scotland

[2] Univ Strathclyde, Strathclyde Inst Pharm & Biomed Sci, 161 Cathedral St, Glasgow G4 0RE, OR, Scotland

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2016年 / 41卷 / 05期

关键词：

MAMMALIAN DIACYLGLYCEROL KINASES; PLASMA-MEMBRANE; DEPENDENT TRANSLOCATION; CELL-PROLIFERATION; CRYSTAL-STRUCTURE; ACTIVATION; BINDING; 1-PHOSPHATE; SPHINGOSINE-1-PHOSPHATE; RECEPTOR;

D O I：

10.1016/j.tibs.2016.02.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Sphingosine kinases (SK1 and SK2) catalyse the conversion of sphingosine into sphingosine 1-phosphate and control fundamental cellular processes, including cell survival, proliferation, differentiation, migration, and immune function. In this review, we highlight recent breakthroughs in the structural and functional characterisation of SKI and these are contextualised by analysis of crystal structures for closely related prokaryotic lipid kinases. We identify a putative dimerisation interface and propose novel regulatory mechanisms governing structural plasticity induced by phosphorylation and interaction with phospholipids and proteins. Our analysis suggests that the catalytic function and regulation of the enzymes might be dependent on conformational mobility and it provides a roadmap for future interrogation of SK1 function and its role in physiology and disease.

引用

收藏

页码：395 / 409

页数：15

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