ArticleThe Biochemical journal1998
LIM domains of cysteine-rich protein 1 (CRP1) are essential for its zyxin-binding function.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Computational analysis of the flexibility in the disordered linker region connecting LIM domains in cysteine-glycine-rich protein.Frontiers in genetics · 2023Article
- Testin protects against cardiac hypertrophy by targeting a calcineurin-dependent signalling pathway.Journal of cellular and molecular medicine · 2019Article
- Cell matrix adhesions in cancer: The proteins that form the glue.Oncotarget · 2017Review
- Human muscle LIM protein dimerizes along the actin cytoskeleton and cross-links actin filaments.Molecular and cellular biology · 2014Article
- Dimensional and temporal controls of three-dimensional cell migration by zyxin and binding partners.Nature communications · 2012Article
- Cysteine- and glycine-rich protein 1a is involved in spinal cord regeneration in adult zebrafish.The European journal of neuroscience · 2012Article
- CRP1, a protein localized in filopodia of growth cones, is involved in dendritic growth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Genes, proteins and complexes: the multifaceted nature of FHL family proteins in diverse tissues.Journal of cellular and molecular medicine · 2010Review
- Zyxin is involved in thrombin signaling via interaction with PAR-1 receptor.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- Transforming growth factor beta up-regulates cysteine-rich protein 2 in vascular smooth muscle cells via activating transcription factor 2.The Journal of biological chemistry · 2008Article
- Identification of Jade1, a gene encoding a PHD zinc finger protein, in a gene trap mutagenesis screen for genes involved in anteroposterior axis development.Molecular and cellular biology · 2003Article
- Targeted disruption of the murine zyxin gene.Molecular and cellular biology · 2003Article
- LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1.The Biochemical journal · 2001Article
- Fine mapping of the alpha-actinin binding site within cysteine-rich protein.The Biochemical journal · 2000Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Previous studies have demonstrated that the adhesion-plaque protein, zyxin, interacts specifically with a 23 kDa protein, called the cysteine-rich protein 1 (CRP1), which has been implicated in myogenesis. Primary sequence analyses have revealed that both zyxin and CRP1 exhibit multiple copies of a structural motif called the LIM domain. LIM domains, which are defined by the consensus CX2CX16-23HX2CX2CX2CX16-23CX2-3(C,H,D), are found in a variety of proteins that are involved in cell growth and differentiation. Recent studies have established that LIM domains are zinc-binding structures that mediate specific protein-protein interactions. For example, in the case of the zyxin-CRP1 interaction, one of zyxin's three LIM domains is necessary and sufficient for binding to CRP1. Because the CRP1 molecule is comprised primarily of two LIM domains, we were interested in the possibility that the binding site for zyxin on CRP1 might also be contained within a single LIM domain. Consistent with the hypothesis that the LIM domains of CRP1 are critical for the protein's zyxin-binding function, zinc-depleted CRP1 displays a reduced zyxin-binding activity. However, domain mapping analyses have revealed that neither of the two individual LIM domains of CRP1 can support a wild-type interaction with zyxin. Collectively, our results suggest that the binding site for zyxin on CRP1 is not contained within a single contiguous sequence of amino acids. Instead, the interaction appears to rely on the co-ordinate action of a number of residues that are displayed in both of CRP1's LIM domains.
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