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Validated All-in-One™ qPCR Primer for LIMK1(NM_002314.3) Search again
Product ID:
HQP010619
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
LIMK, LIMK-1
Gene Description:
LIM domain kinase 1
Target Gene Accession:
NM_002314.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers.
Gene References into function
- Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis.
- identification as interaction partner of 14-3-3 zeta
- LIM kinase 1 (LIMK1), a critical regulator of actin dynamics, plays a regulatory role in tumor cell invasion.
- LIMK1 has a role in regulating cell division and invasive property of prostate cancer cells; the effect is not mediated by phosphorylation of cofilin
- Data suggest that the effect of nuclear LIM kinase on cyclin D1 expression regulates the duration of G1 phase and the degree to which G1 phase progression depends on actin stress fiber formation and imposition of cellular tension.
- LIM-kinase 1 is translocated to the nucleus after being bound by p57kip2
- LIMK1 is enriched in both axonal and dendritic growth cones of E18 hippocampal pyramidal neurons where it is found in punctae that extend far out into filopodia, as well as in a perinuclear region identified as Golgi.
- LIMK1 is cleaved and activated during antiFas antibody-induced apoptosis. Expression of an N-terminally truncated LMK1 fragment induced membrane blebbing.
- LATS1 is a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1.
- a multi-protein complex consisting of SSH-1L, LIMK1, actin, and the scaffolding protein, 14-3-3zeta, is involved, along with the kinase, PAK4, in the regulation of ADF/cofilin activity
- LIMK1 activity is required for thrombin-induced modulation of microtubule destabilization and actin polymerization
- Rnf6 controls cellular LIMK1 concentrations and indicate a new function for the ubiquitin/proteasome system in regulating local growth cone actin dynamics
- results suggested an important role for LIMK1 signaling in breast cancer tumor growth, angiogenesis and invasion and a regulatory connection between LIMK1 and the uPA system
- LIMK1 may play a role different from that of LIMK2 in regulating mitotic spindle organization, chromosome segregation, and cytokinesis during the cell division cycle.
- Elastin and LIMK1 SNPs effect in the at-risk haplotype possibly by weakening the vascular wall and promoting the development of IA
- Taken together, our novel findings presented in this paper implicate that LIMK1 signaling indeed plays a pivotal role in the regulation of EGFR trafficking through the endocytic pathway in invasive tumor cells.
- the structure, regulation and function; possible contributions to human disease (Review)
- These findings demonstrate a cell-type dependent functional interaction between parkin and LIMK1 and provide new evidence that links parkin and LIMK1 in the pathogenesis of familial PD.
- gamma-tubulin associates with phosphorylated LIMK1 and LIMK2 but not with dephosphorylated LIMK1 or LIMK2.
- LIMK1 phosphorylation of p25 blocks p25 activity, thus promoting microtubule disassembly.
- LIMK1-mediated cofilin phosphorylation is required for accurate spindle orientation by stabilizing cortical actin networks during mitosis.
- PDGF participates in actin dynamics by dual regulation of cofilin activity via LIMK and SSH1L in aortic smooth muscle cells
- These results support a model whereby hepatocyte growth factor-stimulated cell migration also requires a cofilin phosphorylation step that is mediated by PAK4.
- LIMK1 may mediate TGF-beta-dependent signaling during ocular inflammation.
