The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.
The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.
复制标题
阳离子通道 mucolipin-1 是一种双功能蛋白，可通过其丝氨酸脂肪酶结构域促进膜重塑。
DOI：
10.1016/j.yexcr.2011.01.008
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发表时间：
2011
影响因子：
3.7
通讯作者：
Vassilev,PeterM
中科院分区：
文献类型：
--
作者：
LaPlante,JaniceM;Falardeau,JohnL;Brown,EdwardM;Slaugenhaupt,SusanA;Vassilev,PeterM
Phospholipase modulators have been shown to affect the topology of lipid bilayers and the formation of tubulo-vesicular structures, but the specific endogenous phospholipases involved have yet to be identified. Here we show that TRPML1 (MLN1), a Ca2+-permeable channel, contributes to membrane remodeling through a serine lipase consensus domain, and thus represents a novel type of bifunctional protein. Remarkably, this serine lipase active site determines the ability of MLN1 to generate tubulo-vesicular extensions in mucolipin-1-expressing oocytes, human fibroblasts and model membrane vesicles. Our demonstration that MLN1 is involved in membrane remodeling and the formation of extensions suggests that it may play a role in the formation of cellular processes linked to the late endosome/lysosome (LE/L) pathway. MLN1 is absent or mutated in patients with mucolipidosis IV (MLIV), a lysosomal disorder with devastating neurological and other consequences. This study provides potential insight into the pathophysiology of MLIV.
