Self‐association of LIM‐kinase 1 mediated by the interaction between an N‐terminal LIM domain and a C‐terminal kinase domain

@article{Hiraoka1996SelfassociationOL,
  title={Self‐association of LIM‐kinase 1 mediated by the interaction between an N‐terminal LIM domain and a C‐terminal kinase domain},
  author={J Hiraoka and I. Okano and Osamu Higuchi and Neng Yang and Kensaku Mizuno},
  journal={FEBS Letters},
  year={1996},
  volume={399}
}
Hsp90 increases LIM kinase activity by promoting its homo‐dimerization
TLDR
It is shown that the half‐life of LIMK1 in cells depends on the presence of active Hsp90, and these findings implicate HSp90 in the stabilization of LimK1 by promoting homodimer formation and transphosphorylation.
Inhibition of neurite extension by overexpression of individual domains of LIM kinase 1
TLDR
The data suggest that the different non‐catalytic N‐terminal domains of LIMK1 contribute to the regulation of neurite extension by using distinct signal transduction pathways.
Cytoplasmic localization of LIM-kinase 1 is directed by a short sequence within the PDZ domain.
TLDR
Results suggest that the PDZ domain, particularly the B region, of LIMK1 has a specific function to localize the protein in the cytoplasm, and probably has nuclear export signal activity.
LIM kinases: function, regulation and association with human disease
TLDR
The LIM kinases have been proposed to play an important role in tumour-cell invasion and metastasis; fine-tuning the balance between phosphorylated and non-phosphorylated cofilin may be a significant determinant of tumours metastatic potential.
Nuclear export of LIM-kinase 1, mediated by two leucine-rich nuclear-export signals within the PDZ domain.
TLDR
It is suggested that the predominant localization of LimK1 in the cytoplasm is supported by two NESs within the PDZ domain and that LIMK1 normally shuttles between the cy toplasm and the nucleus.
Characterization of paxillin LIM domain‐associated serine threonine kinases: Activation by angiotensin II in vascular smooth muscle cells
TLDR
In vivo labeling, phosphoamino acid analysis, and phosphopeptide mapping of paxillin immunoprecipitated from angiotensin II‐stimulated smooth muscle cells confirmed an induction of pXillin serine/threonine phosphorylation and supports the contention that these newly identified paxillins kinases are dynamic components of growth factor signaling through the cytoskeleton.
LIMK2-1, a new isoform of human LIMK2, regulates actin cytoskeleton remodeling via a different signaling pathway than that of its two homologs, LIMK2a and LIMK2b.
TLDR
The data suggest that LIMK2-1 regulates actin cytoskeleton dynamics by preventing PP1-mediated cofilin dephosphorylation, rather than by directly phosphorylating coFilin as its two counterparts, LimK2a and LIMK 2b, may allow for tight regulation of the phospho-cofilin pool, determining the fate of the cell.
Molecular Mechanisms of Beta-Arrestin-1 Dependent Regulation of LIMK and Cofilin
TLDR
R residues in the N-terminus of β-arrestin-1 are involved in LIMK inhibition and cofilin activation and this, in turn, is important for cell migration downstream of PAR-2.
Identification of testis-specific (Limk2t) and brain-specific (Limk2c) isoforms of mouse LIM-kinase 2 gene transcripts.
TLDR
Testis- and brain-specific expression of Limk2t andLimk2c suggests specific roles in these tissues and describes two additional transcripts of the mouse Limk1 gene coding for proteins with distinct N-terminal LIM structures.
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References

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The cysteine‐rich LIM domains inhibit DNA binding by the associated homeodomain in Isl‐1.
TLDR
The ability of LIM domains to inhibit DNA binding by the homeodomains provides a possible basis for negative regulation of LIM‐homeodomain proteins in vivo.
LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family.
TLDR
Rat cDNA clones encoding LIMK-1 and -2 are closely related but distinct members of a novel LIM-containing protein kinase subfamily and are likely to have specific functions in previously uncharacterized signaling pathways.
Identification and Characterization of a Novel Family of Serine/Threonine Kinases Containing Two N-terminal LIM Motifs (*)
TLDR
Immunofluorescence and subcellular fractionation analysis revealed that Myc-tagged LIMK1 and LIMK2 were localized mainly in the cytoplasm, and a 140-kDa tyrosine-phosphorylated protein (pp140) may be a LimK1-associated protein involved in the regulation of LIMK 1 function.
Specificity of LIM Domain Interactions with Receptor Tyrosine Kinases*
TLDR
It is concluded that LIM domains of Enigma recognize tyrosine-containing motifs with specificity residing in both the LIM domains and in the target structures.
AH/PH domain-mediated interaction between Akt molecules and its potential role in Akt regulation
TLDR
Evidence is presented that the AH/PH domain is a domain of protein-protein interaction which mediates the formation of Akt protein complexes and the interaction between c-akt AH/ PH domains is highly specific, as determined by the failure of this domain to bind AKT2.
Specific in vivo association between the bHLH and LIM proteins implicated in human T cell leukemia.
TLDR
This work has found that RBTN1 and RBTN2 have the ability to interact with each of the leukemogenic bHLH proteins (TAL1, TAL2 and LYL1), and identified a subset of leukemia patients that harbor tumor‐specific rearrangements of both their RB TN2 and TAL1 genes.
Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif.
TLDR
Although the protein kinase domain of LIMK has highly conserved sequence elements of protein kinases, phylogenetic analysis revealed that LIMK cannot be classified into any subfamily of known protein kinased, and is suggested to be involved in protein-protein interactions by binding to another LIM motif.
Limk1 is predominantly expressed in neural tissues and phosphorylates serine, threonine and tyrosine residues in vitro.
TLDR
It is demonstrated that GST-Limk1-fusion protein can autophosphorylate on serine, tyrosine and threonine residues in vitro and that mutation of residue D460 within the IHRDL motif abolishes kinase activity.
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