ArticleJournal of biomedical science2013
Ser1333 phosphorylation indicates ROCKI activation.
Article in Journal of biomedical science, 2013. 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.
- Phosphoproteomic Data Integration Reveals Paralog-Specific Co-Regulatory Networks of Rho-Associated Kinases ROCK1 and ROCK2.International journal of molecular sciences · 2026Article
- Multiomics analysis reveals dermokine as a regulator of keratinocyte differentiation and adhesion.JCI insight · 2026Article
- CD20 tails interact with the 14-3-3/GEF-H1 complex and microtubule network upon PKCδ phosphorylation.The EMBO journal · 2026Article
- Total Flavones ofCurrent issues in molecular biology · 2025Article
- Cancer cell response to extrinsic and intrinsic mechanical cue: opportunities for tumor apoptosis strategies.Regenerative biomaterials · 2024Review
- α-Actinin-4 recruits Shp2 into focal adhesions to potentiate ROCK2 activation in podocytes.Life science alliance · 2022Article
- The CDC42 effector protein MRCKβ autophosphorylates on Threonine 1108.Small GTPases · 2020Article
- Discovery of Potent and Selective MRCK Inhibitors with Therapeutic Effect on Skin Cancer.Cancer research · 2018Article
- Article
- The Function of Rho-Associated Kinases ROCK1 and ROCK2 in the Pathogenesis of Cardiovascular Disease.Frontiers in pharmacology · 2015Review
- A novel small-molecule MRCK inhibitor blocks cancer cell invasion.Cell communication and signaling : CCS · 2014Article
- Rho-associated coiled-coil containing kinases (ROCK): structure, regulation, and functions.Small GTPases · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTwo isoforms of Rho-associated protein kinase (ROCK), ROCKI and ROCKII, play a pivotal role in regulation of cytoskeleton and are involved in multiple cellular processes in mammalian cells. Knockout mice experiments have indicated that the functions of ROCKI and II are probably non-redundant in physiology. However, it is difficult to differentiate the activation status of ROCKI and ROCKII in biological samples. Previously, we have identified phosphorylation site of ROCKII at Ser1366 residue sensitive to ROCK inhibition. We further investigated the activity-dependent phosphorylation site in ROCKI to establish the reagents that can be used to detect their individual activation.
resultsThe phosphorylation site of ROCKI sensitive to its inhibition was identified to be the Ser1333 residue. The ROCKI pSer1333-specific antibody does not cross-react with phosphorylated ROCKII. The extent of S1333 phosphorylation of ROCKI correlates with myosin II light chain phosphorylation in cells in response to RhoA stimulation.
conclusionsActive ROCKI is phosphorylated at Ser1333 site. Antibodies that recognize phospho-Ser1333 of ROCKI and phospho-S1366 residues of ROCKII offer a means to discriminate their individual active status in cells and tissues.
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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.