ArticleThe Journal of biological chemistry2009
Smooth muscle archvillin is an ERK scaffolding protein.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Navigating the ERK1/2 MAPK Cascade.Biomolecules · 2023Review
- Supervillin Contributes to LPS-induced Inflammatory Response in THP-1 Cell-derived Macrophages.Inflammation · 2022Article
- Novel γ-sarcoglycan interactors in murine muscle membranes.Skeletal muscle · 2022Article
- Loss of supervillin causes myopathy with myofibrillar disorganization and autophagic vacuoles.Brain : a journal of neurology · 2020Article
- Supervillin promotes epithelial-mesenchymal transition and metastasis of hepatocellular carcinoma in hypoxia via activation of the RhoA/ROCK-ERK/p38 pathway.Journal of experimental & clinical cancer research : CR · 2018Article
- Generation and characterization of monoclonal antibodies that recognize human and murine supervillin protein isoforms.PloS one · 2018Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- Preparation and Affinity-Purification of Supervillin Isoform 4 (SV4) Specific Polyclonal Antibodies.The protein journal · 2016Article
- ERK Signals: Scaffolding Scaffolds?Frontiers in cell and developmental biology · 2016Article
- Cortical actin regulation modulates vascular contractility and compliance in veins.The Journal of physiology · 2015Article
- Gamma-sarcoglycan is required for the response of archvillin to mechanical stimulation in skeletal muscle.Human molecular genetics · 2015Article
- An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.Journal of biomolecular structure & dynamics · 2013Article
- Supervillin-mediated suppression of p53 protein enhances cell survival.The Journal of biological chemistry · 2013Article
- Regulation of PKC autophosphorylation by calponin in contractile vascular smooth muscle tissue.BioMed research international · 2013Article
- Scaffolding proteins and non-proliferative functions of ERK1/2.Communicative & integrative biology · 2010Article
- Novel interactors and a role for supervillin in early cytokinesis.Cytoskeleton (Hoboken, N.J.) · 2010Article
- The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility.Traffic (Copenhagen, Denmark) · 2010Article
- h3/Acidic calponin: an actin-binding protein that controls extracellular signal-regulated kinase 1/2 activity in nonmuscle cells.Molecular biology of the cell · 2010Article
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
ERK influences a number of pathways in all cells, but how ERK activities are segregated between different pathways has not been entirely clear. Using immunoprecipitation and pulldown experiments with domain-specific recombinant fragments, we show that smooth muscle archvillin (SmAV) binds ERK and members of the ERK signaling cascade in a domain-specific, stimulus-dependent, and pathway-specific manner. MEK binds specifically to the first 445 residues of SmAV. B-Raf, an upstream regulator of MEK, constitutively interacts with residues 1-445 and 446-1250. Both ERK and 14-3-3 bind to both fragments, but in a stimulus-specific manner. Phosphorylated ERK is associated only with residues 1-445. An ERK phosphorylation site was determined by mass spectrometry to reside at Ser132. A phospho-antibody raised to this site shows that the site is phosphorylated during alpha-agonist-mediated ERK activation in smooth muscle tissue. Phosphorylation of SmAV by ERK decreases the association of phospho-ERK with SmAV. These results, combined with previous observations, indicate that SmAV serves as a new ERK scaffolding protein and provide a mechanism for regulation of ERK binding, activation, and release from the signaling complex.
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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.