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鉴定一种作为CD36/LIMP-II同源物的盘基网柄菌肌动蛋白结合蛋白缺失表型的抑制因子。

Identification of a suppressor of the Dictyostelium profilin-minus phenotype as a CD36/LIMP-II homologue.

作者信息

Karakesisoglou I, Janssen K P, Eichinger L, Noegel A A, Schleicher M

机构信息

A.-Butenandt-Institut für Zellbiologie, Ludwig-Maximilians-Universität, 80336 München, Germany.

出版信息

J Cell Biol. 1999 Apr 5;145(1):167-81. doi: 10.1083/jcb.145.1.167.

DOI:10.1083/jcb.145.1.167
PMID:10189376
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2148220/
Abstract

Profilin is an ubiquitous G-actin binding protein in eukaryotic cells. Lack of both profilin isoforms in Dictyostelium discoideum resulted in impaired cytokinesis and an arrest in development. A restriction enzyme-mediated integration approach was applied to profilin-minus cells to identify suppressor mutants for the developmental phenotype. A mutant with wild-type-like development and restored cytokinesis was isolated. The gene affected was found to code for an integral membrane glycoprotein of a predicted size of 88 kD containing two transmembrane domains, one at the NH2 terminus and the other at the COOH terminus. It is homologous to mammalian CD36/LIMP-II and represents the first member of this family in D. discoideum, therefore the name DdLIMP is proposed. Targeted disruption of the lmpA gene in the profilin-minus background also rescued the mutant phenotype. Immunofluorescence revealed a localization in vesicles and ringlike structures on the cell surface. Partially purified DdLIMP bound specifically to PIP2 in sedimentation and gel filtration assays. A direct interaction between DdLIMP and profilin could not be detected, and it is unclear how far upstream in a regulatory cascade DdLIMP might be positioned. However, the PIP2 binding of DdLIMP points towards a function via the phosphatidylinositol pathway, a major regulator of profilin.

摘要

肌动蛋白结合蛋白是真核细胞中一种普遍存在的G-肌动蛋白结合蛋白。盘基网柄菌中两种肌动蛋白结合蛋白亚型的缺失导致胞质分裂受损和发育停滞。采用限制酶介导的整合方法对缺失肌动蛋白结合蛋白的细胞进行处理，以鉴定发育表型的抑制突变体。分离出了一个具有野生型样发育且胞质分裂恢复的突变体。发现受影响的基因编码一种预测大小为88 kD的整合膜糖蛋白，该蛋白含有两个跨膜结构域，一个在NH2末端，另一个在COOH末端。它与哺乳动物的CD36/LIMP-II同源，是盘基网柄菌中该家族的第一个成员，因此建议命名为DdLIMP。在缺失肌动蛋白结合蛋白的背景下对lmpA基因进行靶向破坏也挽救了突变体表型。免疫荧光显示其定位于细胞表面的囊泡和环状结构中。在沉降和凝胶过滤试验中，部分纯化的DdLIMP能特异性结合PIP2。未检测到DdLIMP与肌动蛋白结合蛋白之间的直接相互作用，目前尚不清楚DdLIMP在调控级联反应中可能处于上游多远的位置。然而，DdLIMP与PIP2的结合表明其可能通过磷脂酰肌醇途径发挥作用，而磷脂酰肌醇途径是肌动蛋白结合蛋白的主要调节因子。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/f5670ad0df9b/JCB9810076.f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/8f327d0a311c/JCB9810076.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/ebf45fd7d603/JCB9810076.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/f7db0d47dcd5/JCB9810076.f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/a78587f6ded6/JCB9810076.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/4658cb2385ff/JCB9810076.f4a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/8126627ff914/JCB9810076.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/a5eba5a0919d/JCB9810076.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/694a8ba66f01/JCB9810076.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/f5670ad0df9b/JCB9810076.f9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/8f327d0a311c/JCB9810076.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/ebf45fd7d603/JCB9810076.f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/f7db0d47dcd5/JCB9810076.f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/a78587f6ded6/JCB9810076.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/4658cb2385ff/JCB9810076.f4a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/8126627ff914/JCB9810076.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/a5eba5a0919d/JCB9810076.f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/694a8ba66f01/JCB9810076.f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/281f/2148220/f5670ad0df9b/JCB9810076.f9.jpg

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