帕拉丁是真核细胞中整合素连接激酶衔接蛋白的一个新的结合伴侣。

Palladin is a novel binding partner of ILKAP in eukaryotic cells.

机构信息

Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, PR China.

出版信息

Biochem Biophys Res Commun. 2011 Aug 12;411(4):768-73. doi: 10.1016/j.bbrc.2011.07.022. Epub 2011 Jul 18.

DOI:10.1016/j.bbrc.2011.07.022

PMID:21782789

Abstract

Palladin was a novel binding partner of ILKAP in eukaryotic cells. Palladin's C-terminal fragment including only its last three Ig domains (residues 710-1106) and the PP2C domain of ILKAP (residues 108-392) were necessary and sufficient for their interaction. The biological significance of the interaction between palladin and ILKAP was that palladin recruited the cytoplasmic ILKAP to initiate ILKAP-induced apoptosis. Our results suggested that palladin played a specific role in modulating the subcellular localization of the cytoplasmic ILKAP and promoting the ILKAP-induced apoptosis.

摘要

帕拉丁（Palladin）是真核细胞中 ILKAP 的新型结合伴侣。帕拉丁（Palladin）的 C 末端片段仅包含其最后三个 Ig 结构域（残基 710-1106）和 ILKAP 的 PP2C 结构域（残基 108-392），对于它们的相互作用是必需且充分的。帕拉丁（Palladin）和 ILKAP 之间相互作用的生物学意义在于，帕拉丁（Palladin）募集细胞质中的 ILKAP 以启动由 ILKAP 诱导的细胞凋亡。我们的结果表明，帕拉丁（Palladin）在调节细胞质中 ILKAP 的亚细胞定位并促进 ILKAP 诱导的细胞凋亡方面发挥了特定作用。