The LIM domain: from the cytoskeleton to the nucleus

Kadrmas, Julie L.; Beckerle, Mary C.

doi:10.1038/nrm1499

Cited by 679 publications

(711 citation statements)

References 118 publications

Supporting

Mentioning

695

Contrasting

Unclassified

Order By: Relevance

“…Given the presence of an LIM domain emerging as a hallmark of proteins that can associate with both the actincytoskeleton and the transcriptional machinery (Labouesse and Georges-Labouesse, 2003;Kadrmas and Beckerle, 2004), we started our functional characterization on ZNF185 by investigating its intracellular localization. We did not observe a significant localization of either ectopically expressed or endogenous ZNF185 within the nucleus, but instead found that ZNF185 is an actin-cytoskeleton-associated protein.…”

Section: Discussionmentioning

confidence: 99%

“…The LIM domain is a cysteine-and histidine-rich double zinc-finger motif named after the three-homeodomain proteins: Lin-l 1, Isl-1 and Mec-3 (Way and Chalfie, 1988;Freyd et al, 1990;Karlsson et al, 1990). This domain is present in a wide range of proteins whose functions include many fundamental biological processes such as cell lineage specification, cytoskeleton organization and organ development (Dawid et al, 1998;Bach, 2000;Kadrmas and Beckerle, 2004). In addition, some LIM domain-containing proteins are also involved in pathological processes such as oncogenesis (e.g.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

ZNF185, an actin–cytoskeleton-associated growth inhibitory LIM protein in prostate cancer

2006

View full text Add to dashboard Cite

We have recently identified ZNF185 as a gene that is downregulated in prostate cancer (PCa), in part via epigenetic alteration, and maybe associated with disease progression. In this study, we cloned the ZNF185 cDNA from normal human prostate tissues and investigated its biological function. We show that ZNF185 is a novel actin-cytoskeleton-associated Lin-l 1, Isl-1 and Mec-3 (LIM) domain-containing protein that localizes to F-actin structures, and is enriched at focal adhesions. We find that the NH 2 -terminal region, which we designate the actintargeting domain, facilitates ZNF185 binding to actin in vitro and is both necessary and sufficient to mediate actin-cytoskeleton targeting of ZNF185, whereas the LIM domain, which is localized in the COOH-terminus is dispensable for this phenomenon. Interestingly, ectopic expression of full-length ZNF185, but not a mutant lacking the actin-targeting domain, could suppress proliferation and anchorage-independent growth of PCa cells. Together, our data suggest that ZNF185 may function as a tumor-suppressor protein by associating with the actincytoskeleton.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

ZNF185, an actin–cytoskeleton-associated growth inhibitory LIM protein in prostate cancer

2006

View full text Add to dashboard Cite

show abstract

“…Glucose dehydrogenase Recent work has shown that zyxin also shuttles through the nucleus -most likely by association with other LIM proteins -and may regulate gene transcription (Nix et al, 2001;Wang and Gilmore, 2003;Kadrmas and Beckerle, 2004). During mitosis, a fraction of zyxin becomes associated with the tumour suppressor h-warts at the mitotic apparatus (Hirota et al, 2000).…”

Section: -3-3mentioning

confidence: 99%

Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation

Grünewald

Kämmerer

Winkler³

et al. 2007

Br J Cancer

108

135

View full text Add to dashboard Cite

LIM and SH3 protein 1 (LASP-1), initially identified from human breast cancer, is a specific focal adhesion protein involved in cell proliferation and migration. In the present work, we analysed the effect of LASP-1 on biology and function of human ovarian cancer cell line SKOV-3 using small interfering RNA technique (siRNA).Transfection with LASP-1-specific siRNA resulted in a reduced protein level of LASP-1 in SKOV-3 cells. The siRNA-treated cells were arrested in G 2 /M phase of the cell cycle and proliferation of the tumour cells was suppressed by 60 -90% corresponding to around 70% of the cells being transfected successfully as seen by immunofluorescence. Moreover, transfected tumour cells showed a 40% reduced migration. LASP-1 silencing is accompanied by a reduced binding of the LASP-1-binding partner zyxin to focal contacts without changes in actin stress fibre and microtubule organisation or focal adhesion morphology as observed by immunofluorescence. In contrast, silencing of zyxin is not influencing cell migration and had neither influence on LASP-1 expression nor actin cytoskeleton and focal contact morphology suggesting that LASP-1 is necessary and sufficient for recruiting zyxin to focal contacts.The data provide evidence for an essential role of LASP-1 in tumour cell growth and migration, possibly through influencing zyxin localization.

show abstract

“…The LIM domain is a double zinc-fingers in structure and was initially identified in Caenorhabditis elegans Lin-11, rat Isl-1 and C. elegans Mec-3, from which the acronym LIM was derived. 14,15 The LIM protein family can be subdivided into different subfamilies according to sequence homology within the LIM domains, the number of LIM domains and their organization within the proteins. Ajuba belongs to Zyxin/Ajuba subfamily, including Zyxin, Ajuba, Trip6, Wtip, Limd1 and Lpp.…”

mentioning

confidence: 99%

The LIM protein Ajuba promotes adipogenesis by enhancing PPARγ and p300/CBP interaction

Li¹,

Peng

Fan

et al. 2015

Cell Death Differ

View full text Add to dashboard Cite

The LIM domain: from the cytoskeleton to the nucleus

Cited by 679 publications

References 118 publications

ZNF185, an actin–cytoskeleton-associated growth inhibitory LIM protein in prostate cancer

ZNF185, an actin–cytoskeleton-associated growth inhibitory LIM protein in prostate cancer

Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation

The LIM protein Ajuba promotes adipogenesis by enhancing PPARγ and p300/CBP interaction

Contact Info

Product

Resources

About