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迁移细胞中不同信号对细胞收缩和膜皱褶的调节。

Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells.

作者信息

Cheresh D A, Leng J, Klemke R L

机构信息

Departments of Immunology and Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

出版信息

J Cell Biol. 1999 Sep 6;146(5):1107-16. doi: 10.1083/jcb.146.5.1107.

DOI:10.1083/jcb.146.5.1107
PMID:10477763
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2169492/
Abstract

Cell migration and wound contraction requires assembly of actin into a functional myosin motor unit capable of generating force. However, cell migration also involves formation of actin-containing membrane ruffles. Evidence is provided that actin-myosin assembly and membrane ruffling are regulated by distinct signaling pathways in the migratory cell. Interaction of cells with extracellular matrix proteins or cytokines promote cell migration through activation of the MAP kinases ERK1 and ERK2 as well as the molecular coupling of the adaptor proteins p130CAS and c-CrkII. ERK signaling is independent of CAS/Crk coupling and regulates myosin light chain phosphorylation leading to actin-myosin assembly during cell migration and cell-mediated contraction of a collagen matrix. In contrast, membrane ruffling, but not cell contraction, requires Rac GTPase activity and the formation of a CAS/Crk complex that functions in the context of the Rac activating protein DOCK180. Thus, during cell migration ERK and CAS/Crk coupling operate as components of distinct signaling pathways that control actin assembly into myosin motors and membrane ruffles, respectively.

摘要

细胞迁移和伤口收缩需要将肌动蛋白组装成一个能够产生力的功能性肌球蛋白运动单元。然而，细胞迁移还涉及含肌动蛋白的膜皱褶的形成。有证据表明，在迁移细胞中，肌动蛋白-肌球蛋白组装和膜皱褶形成受不同信号通路调控。细胞与细胞外基质蛋白或细胞因子的相互作用通过激活丝裂原活化蛋白激酶ERK1和ERK2以及衔接蛋白p130CAS和c-CrkII的分子偶联来促进细胞迁移。ERK信号传导独立于CAS/Crk偶联，并调节肌球蛋白轻链磷酸化，从而在细胞迁移和细胞介导的胶原基质收缩过程中导致肌动蛋白-肌球蛋白组装。相反，膜皱褶形成（而非细胞收缩）需要Rac GTP酶活性以及在Rac激活蛋白DOCK180背景下起作用的CAS/Crk复合物的形成。因此，在细胞迁移过程中，ERK和CAS/Crk偶联分别作为不同信号通路的组成部分发挥作用，这些信号通路分别控制肌动蛋白组装成肌球蛋白运动单元和膜皱褶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/a45f3ccf5800/JCB9906058.f6c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/666b93040899/JCB9906058.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/733262c63392/JCB9906058.f2a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/2c25432f0769/JCB9906058.f2b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/0c01ba5ef2a3/JCB9906058.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/384dd3df4d7d/JCB9906058.f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/307b4e50f28a/JCB9906058.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/762ebb5a114a/JCB9906058.f6a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/e2503e35363d/JCB9906058.f6b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/a45f3ccf5800/JCB9906058.f6c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/666b93040899/JCB9906058.f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/733262c63392/JCB9906058.f2a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/2c25432f0769/JCB9906058.f2b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/0c01ba5ef2a3/JCB9906058.f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/384dd3df4d7d/JCB9906058.f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/307b4e50f28a/JCB9906058.f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/762ebb5a114a/JCB9906058.f6a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/e2503e35363d/JCB9906058.f6b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d0e7/2169492/a45f3ccf5800/JCB9906058.f6c.jpg

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