ArticleJournal of molecular biology2009
A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein kinase regions of UNC-89 (obscurin) in Caenorhabditis elegans muscle.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 37 citations in OpenAlex.
- The pseudokinase domain PK1 of UNC-89/obscurin is required for mitochondrial morphology and function in C. elegans.Journal of muscle research and cell motility · 2026Article
- Obscurin a localizes near the cell membrane to modulate stress fiber dynamics and cell migration.The Journal of biological chemistry · 2026Article
- The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025Review
- Ultrastructural Analysis Reveals Mitochondrial Placement Independent of Synapse Placement in Fine Caliber C. elegans Neurons.The Journal of comparative neurology · 2024Article
- PK1 fromOpen biology · 2023Article
- Exploring Obscurin and SPEG Kinase Biology.Journal of clinical medicine · 2021Article
- A Region of UNC-89 (Obscurin) Lying between Two Protein Kinase Domains Is a Highly Elastic Spring Required for Proper Sarcomere Organization.Journal of molecular biology · 2020Article
- Double the trouble: giant proteins with dual kinase activity in the heart.Biophysical reviews · 2020Review
- The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Protein phosphatase 2A is crucial for sarcomere organization in Caenorhabditis elegans striated muscle.Molecular biology of the cell · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Obscure functions: the location-function relationship of obscurins.Biophysical reviews · 2017Review
- The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-coil protein, in Caenorhabditis elegans muscle.Molecular biology of the cell · 2016Article
- Binding partners of the kinase domains in Drosophila obscurin and their effect on the structure of the flight muscle.Journal of cell science · 2015Article
- The sarcomeric M-region: a molecular command center for diverse cellular processes.BioMed research international · 2015Review
- Mesodermal gene expression during the embryonic and larval development of the articulate brachiopod Terebratalia transversa.EvoDevo · 2015Article
- An approach for exploring interaction between two proteins in vivo.Frontiers in physiology · 2014Review
- Structure of giant muscle proteins.Frontiers in physiology · 2013Review
- Obscurins: unassuming giants enter the spotlight.IUBMB life · 2013Review
- The kinase domains of obscurin interact with intercellular adhesion proteins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The C. elegans gene unc-89 encodes a set of mostly giant polypeptides (up to 900 kDa) that contain multiple immunoglobulin (Ig) and fibronectin type 3 (Fn3), a triplet of SH3-DH-PH, and two protein kinase domains. The loss of function mutant phenotype and localization of antibodies to UNC-89 proteins indicate that the function of UNC-89 is to help organize sarcomeric A-bands, especially M-lines. Recently, we reported that each of the protein kinase domains interacts with SCPL-1, which contains a CTD-type protein phosphatase domain. Here, we report that SCPL-1 interacts with LIM-9 (FHL), a protein that we first discovered as an interactor of UNC-97 (PINCH) and UNC-96, components of an M-line costamere in nematode muscle. We show that LIM-9 can interact with UNC-89 through its first kinase domain and a portion of unique sequence lying between the two kinase domains. All the interactions were confirmed by biochemical methods. A yeast three-hybrid assay demonstrates a ternary complex between the two protein kinase regions and SCPL-1. Evidence that the UNC-89/SCPL-1 interaction occurs in vivo was provided by showing that over-expression of SCPL-1 results in disorganization of UNC-89 at M-lines. We suggest two structural models for the interactions of SCPL-1 and LIM-9 with UNC-89 at the M-line.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.