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LyGDI，一种新型的 SHIP 相互作用蛋白，是 FcγR 介导的吞噬作用的负调节剂。

LyGDI, a novel SHIP-interacting protein, is a negative regulator of FcγR-mediated phagocytosis.

机构信息

The Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio, United States of America.

出版信息

PLoS One. 2011;6(6):e21175. doi: 10.1371/journal.pone.0021175. Epub 2011 Jun 14.

DOI:10.1371/journal.pone.0021175
PMID:21695085
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3114867/
Abstract

SHIP and SHIP-2 are inositol phosphatases that regulate FcγR-mediated phagocytosis through catalytic as well as non-catalytic mechanisms. In this study we have used two-dimensional fluorescence difference gel electrophoresis (DIGE) analysis to identify downstream signaling proteins that uniquely associate with SHIP or SHIP-2 upon FcγR clustering in human monocytes. We identified LyGDI as a binding partner of SHIP, associating inducibly with the SHIP/Grb2/Shc complex. Immunodepletion and competition experiments with recombinant SHIP domains revealed that Grb2 and the proline-rich domain of SHIP were necessary for SHIP-LyGDI association. Functional studies in primary human monocytes showed that LyGDI sequesters Rac in the cytosol, preventing it from localizing to the membrane. Consistent with this, suppression of LyGDI expression resulted in significantly enhanced FcγR-mediated phagocytosis.

摘要

SHIP 和 SHIP-2 是肌醇磷酸酶，通过催化和非催化机制调节 FcγR 介导的吞噬作用。在这项研究中，我们使用二维荧光差异凝胶电泳 (DIGE) 分析来鉴定在人单核细胞中 FcγR 聚类时，与 SHIP 或 SHIP-2 特异性相关的下游信号蛋白。我们发现 LyGDI 是 SHIP 的结合伴侣，可诱导与 SHIP/Grb2/Shc 复合物结合。用重组 SHIP 结构域进行免疫耗竭和竞争实验表明，Grb2 和 SHIP 的富含脯氨酸结构域是 SHIP-LyGDI 结合所必需的。在原代人单核细胞中的功能研究表明，LyGDI 将 Rac 隔离在细胞质中，防止其定位到膜上。与此一致，抑制 LyGDI 的表达导致 FcγR 介导的吞噬作用显著增强。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/3f9e2438f16f/pone.0021175.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/8cc4ea5f1836/pone.0021175.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/a990d1976ac5/pone.0021175.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/933d5198b058/pone.0021175.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/c5f0d8dfed40/pone.0021175.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/93ad9b573177/pone.0021175.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/3f9e2438f16f/pone.0021175.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/8cc4ea5f1836/pone.0021175.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/a990d1976ac5/pone.0021175.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/933d5198b058/pone.0021175.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/c5f0d8dfed40/pone.0021175.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/93ad9b573177/pone.0021175.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d870/3114867/3f9e2438f16f/pone.0021175.g006.jpg

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