ArticleMolecular biology of the cell2008
A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (Obscurin) in Caenorhabditis elegans.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 50 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
- The high-quality telomere-to-telomere genome assembly of the earthworm (Amynthas aspergillum).Scientific data · 2025Article
- The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025Review
- Protein kinase 2 of the giant sarcomeric protein UNC-89 regulates mitochondrial morphology and function.Communications biology · 2024Article
- Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely movingeLife · 2021Article
- Exploring Obscurin and SPEG Kinase Biology.Journal of clinical medicine · 2021Article
- Deletion of obscurin immunoglobulin domains Ig58/59 leads to age-dependent cardiac remodeling and arrhythmia.Basic research in cardiology · 2020Article
- 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
- Genome and single-cell RNA-sequencing of the earthworm Eisenia andrei identifies cellular mechanisms underlying regeneration.Nature communications · 2020Article
- 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
- Novel obscurins mediate cardiomyocyte adhesion and size via the PI3K/AKT/mTOR signaling pathway.Journal of molecular and cellular cardiology · 2017Article
- Twitchin kinase inhibits muscle activity.Molecular biology of the cell · 2017Article
- 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
- Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans striated muscle.Molecular biology of the cell · 2015Article
- The sarcomeric M-region: a molecular command center for diverse cellular processes.BioMed research international · 2015Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Mutation of the Caenorhabditis elegans gene unc-89 results in disorganization of muscle A-bands. unc-89 encodes a giant polypeptide (900 kDa) containing two protein kinase domains, PK1 and PK2. Yeast two-hybrid screening using a portion of UNC-89 including PK2, yielded SCPL-1 (small CTD phosphatase-like-1), which contains a C terminal domain (CTD) phosphatase type domain. In addition to the PK2 domain, interaction with SCPL-1 required the putative autoinhibitory sequence, and immunoglobulin (Ig) and fibronectin type 3 (Fn3) domains lying N-terminal of the kinase domain. SCPL-1 also interacts with PK1, and it similarly requires the kinase domain and upstream Fn3 and Ig domains. Analogous regions from the two other giant kinases of C. elegans, twitchin and TTN-1, failed to interact with SCPL-1. The interaction between SCPL-1 and either Ig-Fn3-PK2 or Fn3-Ig-PK1 was confirmed by biochemical methods. The scpl-1b promoter is expressed in the same set of muscles as unc-89. Antibodies to SCPL-1 localize to the M-line and a portion of the I-band. Bacterially expressed SCPL-1 proteins have phosphatase activity in vitro with properties similar to previously characterized members of the CTD phosphatase family. RNA interference knockdown results in a defect in the function of egg-laying muscles. These studies suggest a new role for the CTD phosphatase family, that is, in muscle giant kinase signaling.
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