The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Ca2+Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase
Abstract
Somlyo, Andrew P., and Avril V. Somlyo. Ca 2+Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase. Physiol Rev 83: 1325-1358, 2003; 10.1152/physrev.00023.2003.— Ca 2+sensitivity of smooth muscle and nonmuscle myosin II reflects the ratio of activities of myosin light-chain kinase (MLCK) to myosin light-chain phosphatase (MLCP) and is a major, regulated determinant of numerous cellular processes. We conclude that the majority of phenotypes attributed to the monomeric G protein RhoA and mediated by its effector, Rho-kinase (ROK), reflect Ca 2+sensitization: inhibition of myosin II dephosphorylation in the presence of basal (Ca 2+dependent or independent) or increased MLCK activity. We outline the pathway from receptors through trimeric G proteins (Gα q, Gα 12, Gα 13) to activation, by guanine nucleotide exchange factors (GEFs), from GDP · RhoA · GDI to GTP · RhoA and hence to ROK through a mechanism involving association of GEF, RhoA, and ROK in multimolecular complexes at the lipid cell membrane. Specific domains of GEFs interact with trimeric G proteins, and some GEFs are activated by Tyr kinases whose inhibition can inhibit Rho signaling. Inhibition of MLCP, directly by ROK or by phosphorylation of the phosphatase inhibitor CPI-17, increases phosphorylation of the myosin II regulatory light chain and thus the activity of smooth muscle and nonmuscle actomyosin ATPase and motility. We summarize relevant effects of p21-activated kinase, LIM-kinase, and focal adhesion kinase. Mechanisms of Ca 2+desensitization are outlined with emphasis on the antagonism between cGMP-activated kinase and the RhoA/ROK pathway. We suggest that the RhoA/ROK pathway is constitutively active in a number of organs under physiological conditions; its aberrations play major roles in several disease states, particularly impacting on Ca 2+sensitization of smooth muscle in hypertension and possibly asthma and on cancer neoangiogenesis and cancer progression. It is a potentially important therapeutic target and a subject for translational research.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Coussens, L. M., & Werb, Z. (2002) · Nature · doi:10.1038/nature01322 · Cited by 15,111
Krendel, M., Zenke, F. T., & Bokoch, G. M. (2002) · Nature Cell Biology · doi:10.1038/ncb773 · Cited by 669
Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S., & Mizuno, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3577 · Cited by 533
A role for Rho in Ras transformation
Qiu, R. G., Chen, J., McCormick, F., & Symons, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11781 · Cited by 533
Rho family proteins and Ras transformation: the RHOad less traveled gets congested
Zohn, I. M., Campbell, S. L., Khosravi-Far, R., Rossman, K. L., & Der, C. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202181 · Cited by 352
Ren, Y., Li, R., Zheng, Y., & Busch, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34954 · Cited by 295
RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?
Fukuhara, S., Chikumi, H., & Gutkind, J. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204182 · Cited by 219
Glaven, J. A., Whitehead, I., Bagrodia, S., Kay, R., & Cerione, R. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2279 · Cited by 156
Cited by
Alexander, M. R., & Owens, G. K. (2012) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142315 · Cited by 773
Vascular Smooth Muscle Cells and Arterial Stiffening: Relevance in Development, Aging, and Disease
Lacolley, P., Regnault, V., Segers, P., & Laurent, S. (2017) · Physiological Reviews · doi:10.1152/physrev.00003.2017 · Cited by 734
Rho kinase, a promising drug target for neurological disorders
Mueller, B. K., Mack, H., & Teusch, N. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1719 · Cited by 608
Renal Autoregulation in Health and Disease
Carlström, M., Wilcox, C. S., & Arendshorst, W. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00042.2012 · Cited by 485
Apical constriction: A cell shape change that can drive morphogenesis
Sawyer, J. M., Harrell, J. R., Shemer, G., Sullivan-Brown, J., Roh-Johnson, M., & Goldstein, B. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2009.09.009 · Cited by 448
Metadata
- Authors
- SOMLYO, A. P., & SOMLYO, A. V.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2003-10
- Volume
- 83
- Issue
- 4
- Pages
- 1325-1358
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2138742704
- Cited by
- 1,991
- References
- 8
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Ca2+Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase. https://app.cochat.ai/papers/10.1152/physrev.00023.2003
- The paper
- SOMLYO, A. P., & SOMLYO, A. V. (2003). Ca2+Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase. Physiological Reviews. https://doi.org/10.1152/physrev.00023.2003
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.