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Sjl2p通过Ark1p/Prk1p激酶特异性地参与与肌动蛋白动力学密切相关的内吞作用的早期步骤。

Sjl2p is specifically involved in early steps of endocytosis intimately linked to actin dynamics via the Ark1p/Prk1p kinases.

作者信息

Böttcher Claudia, Wicky Sidonie, Schwarz Heinz, Singer-Krüger Birgit

机构信息

University of Stuttgart, Institute for Biochemistry, Pfaffenwaldring 55, D-70569 Stuttgart, Germany.

出版信息

FEBS Lett. 2006 Jan 23;580(2):633-41. doi: 10.1016/j.febslet.2005.12.082. Epub 2006 Jan 3.

Abstract

Sjl2p is one of three yeast phosphoinositide 5'-phosphatases that belong to the conserved family of synaptojanins. Here, we show that Sjl2p is specifically associated with cortical actin patches which aggregate upon loss of the actin-regulating kinases Ark1p and Prk1p. The Sjl2p-containing clumps overlap with clathrin and early endocytic structures generated independently of NSF/Sec18p, but not with endosome- and trans Golgi network-derived membranes. Consistent with the finding that Sjl2p can bind to clathrin heavy chain in vitro, our results suggest that Sjl2p localizes to smooth endocytic vesicles that may be derived from clathrin-coated structures.

摘要

Sjl2p是酵母中三种磷酸肌醇5'-磷酸酶之一,属于保守的突触素家族。在此,我们表明Sjl2p与皮质肌动蛋白斑块特异性相关,这些斑块在肌动蛋白调节激酶Ark1p和Prk1p缺失时会聚集。含有Sjl2p的团块与网格蛋白以及独立于NSF/Sec18p产生的早期内吞结构重叠,但不与内体和反式高尔基体网络衍生的膜重叠。与Sjl2p在体外可与网格蛋白重链结合的发现一致,我们的结果表明Sjl2p定位于可能源自网格蛋白包被结构的光滑内吞小泡。

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