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层粘连蛋白-巢蛋白复合体是跨膜蛋白酪氨酸磷酸酶LAR的一种特定剪接异构体的配体。

The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR.

作者信息

O'Grady P, Thai T C, Saito H

机构信息

Dana-Farber Cancer Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

出版信息

J Cell Biol. 1998 Jun 29;141(7):1675-84. doi: 10.1083/jcb.141.7.1675.

DOI:10.1083/jcb.141.7.1675
PMID:9647658
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2133008/
Abstract

Leukocyte antigen-related protein (LAR) is a prototype for a family of transmembrane protein tyrosine phosphatases whose extracellular domain is composed of three Ig and several fibronectin type III (FnIII) domains. Complex alternative splicing of the LAR-FnIII domains 4-8 has been observed. The extracellular matrix laminin-nidogen complex was identified as a ligand for the LAR-FnIII domain 5 (Fn5) using a series of GST-LAR-FnIII domain fusion proteins and testing them in in vitro ligand-binding assays. LAR- laminin-nidogen binding was regulated by alternative splicing of a small exon within the LAR-Fn5 so that inclusion of this exon sequence resulted in disruption of the laminin-nidogen-binding activity. Long cellular processes were observed when HeLa cells were plated on laminin-nidogen, but not when plated on a fibronectin surface. Indirect immunofluorescent antibody staining revealed high expression of LAR in a punctate pattern, throughout the length of these cellular processes observed on laminin-nidogen. Antibody-induced cross-linking of LAR inhibited formation of these cellular processes, and inhibition was correlated with changes in cellular actin cytoskeletal structure. Thus, LAR-laminin-nidogen binding may play a role in regulating cell signaling induced by laminin-nidogen, resulting in cell morphological changes.

摘要

白细胞抗原相关蛋白（LAR）是一类跨膜蛋白酪氨酸磷酸酶家族的原型，其胞外结构域由三个免疫球蛋白（Ig）和几个纤连蛋白III型（FnIII）结构域组成。已观察到LAR-FnIII结构域4-8存在复杂的可变剪接。利用一系列谷胱甘肽S-转移酶（GST）-LAR-FnIII结构域融合蛋白，并在体外配体结合试验中对其进行测试，确定细胞外基质层粘连蛋白-巢蛋白复合物是LAR-FnIII结构域5（Fn5）的配体。LAR与层粘连蛋白-巢蛋白的结合受LAR-Fn5内一个小外显子可变剪接的调控，因此该外显子序列的包含会导致层粘连蛋白-巢蛋白结合活性的破坏。当HeLa细胞接种在层粘连蛋白-巢蛋白上时可观察到长的细胞突起，而接种在纤连蛋白表面时则没有。间接免疫荧光抗体染色显示，在层粘连蛋白-巢蛋白上观察到的这些细胞突起的全长中，LAR以点状模式高表达。抗体诱导的LAR交联抑制了这些细胞突起的形成，并且抑制作用与细胞肌动蛋白细胞骨架结构的变化相关。因此，LAR与层粘连蛋白-巢蛋白的结合可能在调节由层粘连蛋白-巢蛋白诱导的细胞信号传导中发挥作用，从而导致细胞形态变化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/093a54c82dd1/JCB12582.f8.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/2873440bd6df/JCB12582.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/7da505aa5b9e/JCB12582.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/205502c5239b/JCB12582.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/093a54c82dd1/JCB12582.f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/44f377c1141a/JCB12582.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/fd5e62d4cf1a/JCB12582.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/d94a629c29b1/JCB12582.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/105654781a6d/JCB12582.f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/2873440bd6df/JCB12582.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/7da505aa5b9e/JCB12582.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/205502c5239b/JCB12582.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ae29/2133008/093a54c82dd1/JCB12582.f8.jpg

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本文引用的文献

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Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment.通过可变剪接的EDA片段对纤连蛋白细胞黏附活性的调节。
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白细胞共同抗原相关受体（LAR）的罕见错义变体在跨细胞粘附和突触形成中表现出活性降低。
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The tyrosine phosphatases LAR and PTPRδ act as receptors of the nidogen-tetanus toxin complex.酪氨酸磷酸酶 LAR 和 PTPRδ 作为连接蛋白-破伤风毒素复合物的受体。
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