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PMID: 22744749 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions.

Cellular and molecular life sciences : CMLS ·Vol. 69 ·No. 22 ·2012-11-00 ·Pages 3765-805

Hota PK, Buck M

Abstract

Plexin transmembrane receptors and their semaphorin ligands, as well as their co-receptors (Neuropilin, Integrin, VEGFR2, ErbB2, and Met kinase) are emerging as key regulatory proteins in a wide variety of developmental, regenerative, but also pathological processes. The diverse arenas of plexin function are surveyed, including roles in the nervous, cardiovascular, bone and skeletal, and immune systems. Such different settings require considerable specificity among the plexin and semaphorin family members which in turn are accompanied by a variety of cell signaling networks. Underlying the latter are the mechanistic details of the interactions and catalytic events at the molecular level. Very recently, dramatic progress has been made in solving the structures of plexins and of their complexes with associated proteins. This molecular level information is now suggesting detailed mechanisms for the function of both the extracellular as well as the intracellular plexin regions. Specifically, several groups have solved structures for extracellular domains for plexin-A2, -B1, and -C1, many in complex with semaphorin ligands. On the intracellular side, the role of small Rho GTPases has been of particular interest. These directly associate with plexin and stimulate a GTPase activating (GAP) function in the plexin catalytic domain to downregulate Ras GTPases. Structures for the Rho GTPase binding domains have been presented for several plexins, some with Rnd1 bound. The entire intracellular domain structure of plexin-A1, -A3, and -B1 have also been solved alone and in complex with Rac1. However, key aspects of the interplay between GTPases and plexins remain far from clear. The structural information is helping the plexin field to focus on key questions at the protein structural, cellular, as well as organism level that collaboratoria of investigations are likely to answer.

MeSH Terms
Cardiovascular Diseases Cardiovascular System/embryology,injuries,metabolism Cell Adhesion Molecules/chemistry,metabolism Humans Ligands Neoplasm Metastasis Neoplasms/metabolism Nerve Tissue Proteins/chemistry,metabolism Nervous System/embryology,metabolism Nervous System Diseases/metabolism Semaphorins/chemistry,metabolism Signal Transduction
Chemicals
Cell Adhesion Molecules Ligands Nerve Tissue Proteins Semaphorins plexin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hota Prasanta K
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Buck Matthias
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Article Info
Journal
Cellular and molecular life sciences : CMLS
Abbr.
Cell Mol Life Sci
ISSN
1420-9071
DOI
10.1007/s00018-012-1019-0
Published
2012-11-00
Epub
2012-00-29
Pages
3765-805
Language
English
Region
Switzerland
NLM ID
9705402
Subset
IM
Grants
NIGMS NIH HHS · GM073071 · United States
External Links
PubMed source DOI: 10.1007/s00018-012-1019-0 View journal details
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