ArticleBMC cell biology2009
Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin.
Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- The PDLIM family of actin-associated proteins and their emerging role in membrane trafficking.Biochemical Society transactions · 2023Review
- PDLIM3 supports hedgehog signaling in medulloblastoma by facilitating cilia formation.Cell death and differentiation · 2023Article
- Article
- The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022Review
- Integrated Quantitative Phosphoproteomics and Cell-based Functional Screening Reveals Specific Pathological Cardiac Hypertrophy-related Phosphorylation Sites.Molecules and cells · 2021Article
- Characterizing the actin-binding ability of Zasp52 and its contribution to myofibril assembly.PloS one · 2020Article
- Expression and Purification of ZASP Subdomains and Clinically Important Isoforms: High-Affinity Binding to G-Actin.Biochemistry · 2017Article
- Zasp52, a Core Z-disc Protein in Drosophila Indirect Flight Muscles, Interacts with α-Actinin via an Extended PDZ Domain.PLoS genetics · 2016Article
- Alp/Enigma family proteins cooperate in Z-disc formation and myofibril assembly.PLoS genetics · 2013Article
- Article
- Actin cytoskeleton remodeling by the alternatively spliced isoform of PDLIM4/RIL protein.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, alpha-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown.
resultsIn this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107-273) was largely unfolded in solution, but was able to interact with the alpha-actinin rod domain in vitro, and to co-localize with alpha-actinin on stress fibres in vivo. NMR analysis revealed that the titration of ALP with the alpha-actinin rod domain induces stabilization of ALP. A synthetic peptide (residues 175-196) that contained the N-terminal half of the ZM motif was found to interact directly with the alpha-actinin rod domain in surface plasmon resonance (SPR) measurements. Short deletions at or before the ZM motif abrogated the localization of ALP to actin stress fibres.
conclusionThe internal region of ALP appeared to be largely unstructured but functional. The ZM motif defined part of the interaction surface between ALP and the alpha-actinin rod domain.
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