scholarly journals Mystique Is a New Insulin-like Growth Factor-I-regulated PDZ-LIM Domain Protein That Promotes Cell Attachment and Migration and Suppresses Anchorage-independent Growth

2005 ◽  
Vol 16 (4) ◽  
pp. 1811-1822 ◽  
Author(s):  
Gary Loughran ◽  
Nollaig C. Healy ◽  
Patrick A. Kiely ◽  
Merei Huigsloot ◽  
Nancy L. Kedersha ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Growth Factor ◽  
Epithelial Cells ◽  
Colony Formation ◽  
Insulin Like Growth Factor ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein ◽  
And Migration ◽  
Mcf 7

By comparing differential gene expression in the insulin-like growth factor (IGF)-IR null cell fibroblast cell line (R– cells) with cells overexpressing the IGF-IR (R+ cells), we identified the Mystique gene expressed as alternatively spliced variants. The human homologue of Mystique is located on chromosome 8p21.2 and encodes a PDZ LIM domain protein (PDLIM2). GFP-Mystique was colocalized at cytoskeleton focal contacts with α-actinin and β1-integrin. Only one isoform of endogenous human Mystique protein, Mystique 2, was detected in cell lines. Mystique 2 was more abundant in nontransformed MCF10A breast epithelial cells than in MCF-7 breast carcinoma cells and was induced by IGF-I and cell adhesion. Overexpression of Mystique 2 in MCF-7 cells suppressed colony formation in soft agarose and enhanced cell adhesion to collagen and fibronectin. Point mutation of either the PDZ or LIM domain was sufficient to reverse suppression of colony formation, but mutation of the PDZ domain alone was sufficient to abolish enhanced adhesion. Knockdown of Mystique 2 with small interfering RNA abrogated both adhesion and migration in MCF10A and MCF-7 cells. The data indicate that Mystique is an IGF-IR–regulated adapter protein located at the actin cytoskeleton that is necessary for the migratory capacity of epithelial cells.

Synemin interacts with the LIM domain protein zyxin and is essential for cell adhesion and migration

2010 ◽  
Vol 316 (3) ◽  
pp. 491-505 ◽  
Author(s):  
Ning Sun ◽  
Ted W. Huiatt ◽  
Denise Paulin ◽  
Zhenlin Li ◽  
Richard M. Robson
Keyword(s):  
Cell Adhesion ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Cell Adhesion And Migration ◽  
Domain Protein ◽  
And Migration

The small GTPase Rap1 promotes cell movement rather than stabilizes adhesion in epithelial cells responding to insulin-like growth factor I

2014 ◽  
Vol 463 (2) ◽  
pp. 257-270 ◽  
Author(s):  
Marina A. Guvakova ◽  
William S. Y. Lee ◽  
Dana K. Furstenau ◽  
Indira Prabakaran ◽  
David C. Li ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Adhesion ◽  
Growth Factor ◽  
Epithelial Cells ◽  
Cell Movement ◽  
Supporting Cell ◽  
Small Gtpase ◽  
Insulin Like Growth Factor ◽  
New Paradigm ◽  
Factor I

The present study provides evidence to support a new paradigm for understanding how the labile function of the small GTPase Rap1 is switched from supporting cell adhesion to promoting cell migration.

scholarly journals Ajuba is required for Rac activation and maintenance of E-cadherin adhesion

2011 ◽  
Vol 195 (5) ◽  
pp. 855-871 ◽  
Author(s):  
Sébastien Nola ◽  
Reiko Daigaku ◽  
Kasia Smolarczyk ◽  
Maryke Carstens ◽  
Belen Martin-Martin ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Feedback Loop ◽  
Small Gtpase ◽  
Lim Domain ◽  
Actin Remodeling ◽  
Lim Domain Protein ◽  
Domain Protein ◽  
Pak1 Activation ◽  
E Cadherin ◽  
Cell Cell

Maintenance of stable E-cadherin–dependent adhesion is essential for epithelial function. The small GTPase Rac is activated by initial cadherin clustering, but the precise mechanisms underlying Rac-dependent junction stabilization are not well understood. Ajuba, a LIM domain protein, colocalizes with cadherins, yet Ajuba function at junctions is unknown. We show that, in Ajuba-depleted cells, Rac activation and actin accumulation at cadherin receptors was impaired, and junctions did not sustain mechanical stress. The Rac effector PAK1 was also transiently activated upon cell–cell adhesion and directly phosphorylated Ajuba (Thr172). Interestingly, similar to Ajuba depletion, blocking PAK1 activation perturbed junction maintenance and actin recruitment. Expression of phosphomimetic Ajuba rescued the effects of PAK1 inhibition. Ajuba bound directly to Rac·GDP or Rac·GTP, but phosphorylated Ajuba interacted preferentially with active Rac. Rather than facilitating Rac recruitment to junctions, Ajuba modulated Rac dynamics at contacts depending on its phosphorylation status. Thus, a Rac–PAK1–Ajuba feedback loop integrates spatiotemporal signaling with actin remodeling at cell–cell contacts and stabilizes preassembled cadherin complexes.

Proteomic identification of the LIM domain protein FHL1 as the gene-product mutated in reducing body myopathy

2009 ◽  
Vol 40 (01) ◽  
Author(s):  
J Schessl ◽  
Y Zou ◽  
MJ McGrath ◽  
BS Cowling ◽  
B Maiti ◽  
...  
Keyword(s):  
Gene Product ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Proteomic Identification ◽  
Domain Protein

scholarly journals Four-and-a-half LIM domain protein 2 (FHL2) deficiency protects mice from diet-induced obesity and high FHL2 expression marks human obesity

Metabolism ◽  
2021 ◽  
pp. 154815
Author(s):  
Maria P. Clemente-Olivo ◽  
Jayron J. Habibe ◽  
Mariska Vos ◽  
Roelof Ottenhoff ◽  
Aldo Jongejan ◽  
...  
Keyword(s):  
Lim Domain ◽  
Human Obesity ◽  
Diet Induced Obesity ◽  
Lim Domain Protein ◽  
Domain Protein

scholarly journals The LIM domain protein nTRIP6 modulates the dynamics of myogenic differentiation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tannaz Norizadeh Abbariki ◽  
Zita Gonda ◽  
Denise Kemler ◽  
Pavel Urbanek ◽  
Tabea Wagner ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Satellite Cells ◽  
Muscle Regeneration ◽  
Myogenic Differentiation ◽  
Skeletal Muscle Regeneration ◽  
Temporal Control ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein

AbstractThe process of myogenesis which operates during skeletal muscle regeneration involves the activation of muscle stem cells, the so-called satellite cells. These then give rise to proliferating progenitors, the myoblasts which subsequently exit the cell cycle and differentiate into committed precursors, the myocytes. Ultimately, the fusion of myocytes leads to myofiber formation. Here we reveal a role for the transcriptional co-regulator nTRIP6, the nuclear isoform of the LIM-domain protein TRIP6, in the temporal control of myogenesis. In an in vitro model of myogenesis, the expression of nTRIP6 is transiently up-regulated at the transition between proliferation and differentiation, whereas that of the cytosolic isoform TRIP6 is not altered. Selectively blocking nTRIP6 function results in accelerated early differentiation followed by deregulated late differentiation and fusion. Thus, the transient increase in nTRIP6 expression appears to prevent premature differentiation. Accordingly, knocking out the Trip6 gene in satellite cells leads to deregulated skeletal muscle regeneration dynamics in the mouse. Thus, dynamic changes in nTRIP6 expression contributes to the temporal control of myogenesis.

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