ArticleJournal of molecular biology2009
Characterization of tightly associated smooth muscle myosin-myosin light-chain kinase-calmodulin complexes.
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 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Intracellular tension sensor reveals mechanical anisotropy of the actin cytoskeleton.Nature communications · 2023Article
- Review
- Self-assembly of smooth muscle myosin filaments: adaptation of filament length by telokin and Mg·ATP.European biophysics journal : EBJ · 2022Article
- The myosin light-chain kinase MLCK-1 relocalizes during Caenorhabditis elegans ovulation to promote actomyosin bundle assembly and drive contraction.Molecular biology of the cell · 2018Article
- S-Nitrosoglutathione Reductase Underlies the Dysfunctional Relaxation to Nitric Oxide in Preterm Labor.Scientific reports · 2018Article
- Article
- Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.Cell biochemistry and function · 2016Article
- Diffusion of myosin light chain kinase on actin: A mechanism to enhance myosin phosphorylation rates in smooth muscle.The Journal of general physiology · 2015Article
- Ca(2+) signaling in arterioles and small arteries of conscious, restrained, optical biosensor mice.Frontiers in physiology · 2014Article
- Kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system.Biochemistry · 2013Article
- Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011Review
- Biochemistry of smooth muscle myosin light chain kinase.Archives of biochemistry and biophysics · 2011Review
- In vivo assessment of artery smooth muscle [Ca2+]i and MLCK activation in FRET-based biosensor mice.American journal of physiology. Heart and circulatory physiology · 2010Article
- Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
A current popular model to explain phosphorylation of smooth muscle myosin (SMM) by myosin light-chain kinase (MLCK) proposes that MLCK is bound tightly to actin but weakly to SMM. We found that MLCK and calmodulin (CaM) co-purify with unphosphorylated SMM from chicken gizzard, suggesting that they are tightly bound. Although the MLCK:SMM molar ratio in SMM preparations was well below stoichiometric (1:73+/-9), the ratio was approximately 23-37% of that in gizzard tissue. Fifteen to 30% of MLCK was associated with CaM at approximately 1 nM free [Ca(2+)]. There were two MLCK pools that bound unphosphorylated SMM with K(d) approximately 10 and 0.2 microM and phosphorylated SMM with K(d) approximately 20 and 0.2 microM. Using an in vitro motility assay to measure actin sliding velocities, we showed that the co-purifying MLCK-CaM was activated by Ca(2+) and phosphorylation of SMM occurred at a pCa(50) of 6.1 and at a Hill coefficient of 0.9. Similar properties were observed from reconstituted MLCK-CaM-SMM. Using motility assays, co-sedimentation assays, and on-coverslip enzyme-linked immunosorbent assays to quantify proteins on the motility assay coverslip, we provide strong evidence that most of the MLCK is bound directly to SMM through the telokin domain and some may also be bound to both SMM and to co-purifying actin through the N-terminal actin-binding domain. These results suggest that this MLCK may play a role in the initiation of contraction.
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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.