Literature DB >> 22555291

The MRL proteins: adapting cell adhesion, migration and growth.

Georgina P Coló1, Esther M Lafuente, Joaquin Teixidó.   

Abstract

MIG-10, RIAM and Lamellipodin (Lpd) are the founding members of the MRL family of multi-adaptor molecules. These proteins have common domain structures but display distinct functions in cell migration and adhesion, signaling, and in cell growth. The binding of RIAM with active Rap1 and with talin provides these MRL molecules with important regulatory roles on integrin-mediated cell adhesion and migration. Furthermore, RIAM and Lpd can regulate actin dynamics through their binding to actin regulatory Ena/VASP proteins. Recent data generated with the Drosophila MRL ortholog called Pico and with RIAM in melanoma cells indicate that these proteins can also regulate cell growth. As MRL proteins represent a relatively new family, many questions on their structure-function relationships remain unanswered, including regulation of their expression, post-translational modifications, new interactions, involvement in signaling and their knockout mice phenotype.
Copyright © 2012 Elsevier GmbH. All rights reserved.

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Year:  2012        PMID: 22555291     DOI: 10.1016/j.ejcb.2012.03.001

Source DB:  PubMed          Journal:  Eur J Cell Biol        ISSN: 0171-9335            Impact factor:   4.492


  19 in total

1.  MIG-10 (lamellipodin) has netrin-independent functions and is a FOS-1A transcriptional target during anchor cell invasion in C. elegans.

Authors:  Zheng Wang; Qiuyi Chi; David R Sherwood
Journal:  Development       Date:  2014-02-19       Impact factor: 6.868

2.  MIG-10 (Lamellipodin) stabilizes invading cell adhesion to basement membrane and is a negative transcriptional target of EGL-43 in C. elegans.

Authors:  Lin Wang; Wanqing Shen; Shijun Lei; David Matus; David Sherwood; Zheng Wang
Journal:  Biochem Biophys Res Commun       Date:  2014-08-19       Impact factor: 3.575

3.  Structural and mechanistic insights into the recruitment of talin by RIAM in integrin signaling.

Authors:  Yu-Chung Chang; Hao Zhang; Janusz Franco-Barraza; Mark L Brennan; Tejash Patel; Edna Cukierman; Jinhua Wu
Journal:  Structure       Date:  2014-11-20       Impact factor: 5.006

4.  PtdIns(3,4)P2, Lamellipodin, and VASP coordinate actin dynamics during phagocytosis in macrophages.

Authors:  Fernando Montaño-Rendón; Glenn F W Walpole; Matthias Krause; Gerald R V Hammond; Sergio Grinstein; Gregory D Fairn
Journal:  J Cell Biol       Date:  2022-09-27       Impact factor: 8.077

5.  Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling.

Authors:  Yu-Chung Chang; Hao Zhang; Mark L Brennan; Jinhua Wu
Journal:  Protein Cell       Date:  2013-03-13       Impact factor: 14.870

Review 6.  The Rap1-RIAM-talin axis of integrin activation and blood cell function.

Authors:  Frederic Lagarrigue; Chungho Kim; Mark H Ginsberg
Journal:  Blood       Date:  2016-05-20       Impact factor: 22.113

7.  Loss of the Rap1 effector RIAM results in leukocyte adhesion deficiency due to impaired β2 integrin function in mice.

Authors:  Sarah Klapproth; Markus Sperandio; Elaine M Pinheiro; Monika Prünster; Oliver Soehnlein; Frank B Gertler; Reinhard Fässler; Markus Moser
Journal:  Blood       Date:  2015-09-03       Impact factor: 22.113

Review 8.  Talins and kindlins: partners in integrin-mediated adhesion.

Authors:  David A Calderwood; Iain D Campbell; David R Critchley
Journal:  Nat Rev Mol Cell Biol       Date:  2013-07-17       Impact factor: 94.444

9.  Two modes of integrin activation form a binary molecular switch in adhesion maturation.

Authors:  Ho-Sup Lee; Praju Anekal; Chinten James Lim; Chi-Chao Liu; Mark H Ginsberg
Journal:  Mol Biol Cell       Date:  2013-03-06       Impact factor: 4.138

10.  Lamellipodin tunes cell migration by stabilizing protrusions and promoting adhesion formation.

Authors:  Georgi Dimchev; Behnam Amiri; Ashley C Humphries; Matthias Schaks; Vanessa Dimchev; Theresia E B Stradal; Jan Faix; Matthias Krause; Michael Way; Martin Falcke; Klemens Rottner
Journal:  J Cell Sci       Date:  2020-04-09       Impact factor: 5.285

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