Phosphatidylinositol 3-phosphate recognition by the FYVE domain

被引：143
作者：
Kutateladze, TG
Ogburn, KD
Watson, WT
de Beer, T
Emr, SD
Burd, CG
Overduin, M
机构：
[1] Univ Colorado, Hlth Sci Ctr, Dept Pharmacol, Denver, CO 80262 USA
[2] Univ Penn, Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA
[3] Univ Penn, Sch Med, Inst Human Gene Therapy, Philadelphia, PA 19104 USA
[4] Univ Calif San Diego, Howard Hughes Med Inst, Div Cellular & Mol Med, Sch Med, La Jolla, CA 92093 USA
来源：
MOLECULAR CELL | 1999年 / 3卷 / 06期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/S1097-2765(01)80013-7
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：
Recognition of phosphatidylinositol 3-phosphate (Ptdlns(3)P) is crucial for a broad range of cellular signaling and membrane trafficking events regulated by phosphoinositide (Pl) 3-kinases. Ptdlns(3)P binding by the FYVE domain of human early endosome autoantigen 1 (EEA1), a protein implicated in endosome fusion, involves two beta hairpins and an a helix. Specific amino acids, including those of the FYVE domain's conserved RRHHCRQCGNIF motif, contact soluble and micelle-embedded lipid and provide specificity for Ptdlns(3)P over Ptdlns(5)P and Ptdlns, as shown by heteronuclear magnetic resonance spectroscopy. Although the FYVE domain relies on a zinc-binding motif reminiscent of RING fingers, it is distinguished by novel structural features and its Ptdlns(3)P-binding site.
引用
收藏
页码：805 / 811
页数：7
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