gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

LIM domain and actin binding 1

EPLIN, Epithelial protein lost in neoplasm, Lima-1, epithelial protein lost in neoplasm beta EPLIN
This gene encodes a cytoskeleton-associated protein that inhibits actin filament depolymerization and cross-links filaments in bundles. It is downregulated in some cancer cell lines. Alternatively spliced transcript variants encoding different isoforms have been described for this gene, and expression of some of the variants maybe independently regulated. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: Actin, LIM, CAN, V1a, iMpact
Papers using EPLIN antibodies
EPLIN regulates actin dynamics by cross-linking and stabilizing filaments
Chang David D. et al., In The Journal of Cell Biology, 1996
... The coding region of EPLIN-α and -β was excised from the pCMV-FlagEPLIN plasmids (Maul and Chang, 1999) and cloned into the pTRE vector (CLONTECH Laboratories, Inc.) ...
Papers on EPLIN
Integrative proteomics and transcriptomics identify novel invasive-related biomarkers of non-functioning pituitary adenomas.
Zhang et al., Beijing, China. In Tumour Biol, Feb 2016
Eight genes were identified involved in the invasion function by the molecular and cellular functions analysis, including CAT, CLU, CHGA, EZR, KRT8, LIMA1, SH3GLB2 and SLC2A1.
EPLIN: a fundamental actin regulator in cancer metastasis?
Sanders et al., Cardiff, United Kingdom. In Cancer Metastasis Rev, Dec 2015
Epithelial protein lost in neoplasm (EPLIN) is an actin-associated molecule which has been implicated in the development and progression of various cancers including breast, prostate, oesophageal and lung where EPLIN expression is frequently lost as the cancer progresses.
Proteomic analysis reveals novel common genes modulated in both replicative and stress-induced senescence.
Faraonio et al., Napoli, Italy. In J Proteomics, Nov 2015
We also performed functional studies by silencing nine of these genes in young cells, which demonstrated that RNA interference-mediated knockdown of LEPRE1, LIMA1/EPLIN, MAGOHA and MAGOHB induces a premature senescent phenotype in IMR90 cells.
SATB2 enhances migration and invasion in osteosarcoma by regulating genes involved in cytoskeletal organization.
Irwin et al., Toronto, Canada. In Oncogene, Jul 2015
Microarray analysis identified genes that were differentially regulated by SATB2 including the actin-binding protein Epithelial Protein Lost In Neoplasm (EPLIN), which was upregulated in sh-SATB2 cells.
The focal adhesion protein PINCH-1 associates with EPLIN at integrin adhesion sites.
Fässler et al., Martinsried, Germany. In J Cell Sci, Apr 2015
By isolating the PINCH-1 interactome, the LIM-domain-containing and actin-binding protein epithelial protein lost in neoplasm (EPLIN, also known as LIMA1) was identified as a new PINCH-1-associated protein.
EPLIN is a crucial regulator for extrusion of RasV12-transformed cells.
Fujita et al., Sapporo, Japan. In J Cell Sci, Mar 2015
Here, we demonstrate that Cav-1-containing microdomains and EPLIN (also known as LIMA1) are accumulated in RasV12-transformed cells that are surrounded by normal cells.
Combined comparative genomic hybridization and transcriptomic analyses of ovarian granulosa cell tumors point to novel candidate driver genes.
Veitia et al., Paris, France. In Bmc Cancer, 2014
Many of these genes, such as AKT1, RUNX1 and LIMA1, are known to be involved in cancer and related processes.
Conversion of the LIMA1 tumour suppressor into an oncogenic LMO-like protein by API2-MALT1 in MALT lymphoma.
Elenitoba-Johnson et al., Ann Arbor, United States. In Nat Commun, 2014
Here we show that API2-MALT1 induces paracaspase-mediated cleavage of the tumour suppressor protein LIMA1.
Epithelial protein lost in neoplasm modulates platelet-derived growth factor-mediated adhesion and motility of mesangial cells.
Igarashi et al., Tokyo, Japan. In Kidney Int, 2014
Here we found high expression of the actin cross-linking protein EPLIN (epithelial protein lost in neoplasm) in mesangial cells.
Dynamics between actin and the VE-cadherin/catenin complex: novel aspects of the ARP2/3 complex in regulation of endothelial junctions.
Schnittler et al., Münster, Germany. In Cell Adh Migr, 2013
The functional connection between the cadherin/catenin complex and actin filaments might be either directly through ?-catenins, or indirectly e.g., via linker proteins such as vinculin, p120ctn, ?-actinin, or EPLIN.
DNp73 exerts function in metastasis initiation by disconnecting the inhibitory role of EPLIN on IGF1R-AKT/STAT3 signaling.
Pützer et al., Rostock, Germany. In Cancer Cell, 2013
We provide mechanistic insight toward regulation of LIMA1/EPLIN by p73/DNp73 and demonstrate a direct link between the DNp73-EPLIN axis and IGF1R-AKT/STAT3 activation.
Mechanotransduction at the basis of endothelial barrier function.
Gulino-Debrac, Grenoble, France. In Tissue Barriers, 2013
More particularly, we report on the emerging role of α-catenin and EPLIN that act as a mechanotransmitter of myosin-IIgenerated traction forces.
Epidermal growth factor promotes protein degradation of epithelial protein lost in neoplasm (EPLIN), a putative metastasis suppressor, during epithelial-mesenchymal transition.
Wu et al., Atlanta, United States. In J Biol Chem, 2013
Interestingly, EGF was found to be capable of promoting protein turnover of epithelial protein lost in neoplasm (EPLIN), a putative suppressor of EMT and tumor metastasis.
MicroRNA profiling with correlation to gene expression revealed the oncogenic miR-17-92 cluster to be up-regulated in osteosarcoma.
Nathrath et al., Basel, Switzerland. In Cancer Genet, 2012
In addition, several genes involved in differentiation (RGMB, LRRC17), cell cycle control (CCNE1), and apoptosis (LIMA1, CAMK2N1) were found to be deregulated in osteosarcoma cell lines, most likely due to altered miRNA expression patterns.
EPLIN-α expression in human oesophageal cancer and its impact on cellular aggressiveness and clinical outcome.
Jiang et al., Cardiff, United Kingdom. In Anticancer Res, 2012
Together with the findings that EPLIN-alpha inhibits cellular growth and invasion, we conclude that EPLIN-alpha is a tumour suppressor of oesophageal cancer
Epithelial protein lost in neoplasm (EPLIN) interacts with α-catenin and actin filaments in endothelial cells and stabilizes vascular capillary network in vitro.
Gulino-Debrac et al., Grenoble, France. In J Biol Chem, 2012
EPLIN clutch is necessary for stabilization of capillary structures in an angiogenesis model.
EPLIN downregulation promotes epithelial-mesenchymal transition in prostate cancer cells and correlates with clinical lymph node metastasis.
Wu et al., Atlanta, United States. In Oncogene, 2012
EPLIN downregulation promotes epithelial-mesenchymal transition in prostate cancer cells and correlates with clinical lymph node metastasis.
The impact of EPLINα (Epithelial protein lost in neoplasm) on endothelial cells, angiogenesis and tumorigenesis.
Jiang et al., Cardiff, United Kingdom. In Angiogenesis, 2010
EPLINalpha over-expression can regulate HECV cell motility, matrix adhesion and tubule formation in vitro and slow in vivo tumour formation, suggesting an anti-angiogenic role for EPLINalpha.
The actin-binding and bundling protein, EPLIN, is required for cytokinesis.
Khanna et al., Brisbane, Australia. In Cell Cycle, 2009
EPLIN protein may function during cytokinesis to maintain local accumulation of key cytokinesis proteins at the furrow.
share on facebooktweetadd +1mail to friends