ArticleMolecular endocrinology (Baltimore, Md.)2009
Adapter protein SH2B1beta cross-links actin filaments and regulates actin cytoskeleton.
Article in Molecular endocrinology (Baltimore, Md.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Centrosomal JAK2 Tyrosine Kinase Regulates Primary Cilia Length, Cell Proliferation, and Cilia Orientation During Cell Migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Identification of βIIΣ1-Spectrin as a Binding Partner of the GH-regulated Human Obesity Scaffold Protein SH2B1.Endocrinology · 2025Article
- Endogenous SH2B1 protein localizes to lamellipodia and filopodia: platinum replica electron-microscopy study.microPublication biology · 2025Article
- Exogenous growth hormone promotes an epithelial-mesenchymal hybrid phenotype in cancerous HeLa cells but not in non-cancerous HEK293 cells.Molecular and cellular biochemistry · 2023Article
- miRNAs as Predictors of Barrier Integrity.Biosensors · 2023Review
- The nucleolar δ isoform of adapter protein SH2B1 enhances morphological complexity and function of cultured neurons.Journal of cell science · 2022Article
- Deletion of the Brain-Specific α and δ Isoforms of Adapter Protein SH2B1 Protects Mice From Obesity.Diabetes · 2021Article
- Genetic Association ofDiabetes, metabolic syndrome and obesity : targets and therapy · 2020Article
- SH2B1 promotes epithelial-mesenchymal transition through the IRS1/β-catenin signaling axis in lung adenocarcinoma.Molecular carcinogenesis · 2018Article
- MicroRNA-361-3p suppresses tumor cell proliferation and metastasis by directly targeting SH2B1 in NSCLC.Journal of experimental & clinical cancer research : CR · 2016Article
- SH2B1 and IRSp53 proteins promote the formation of dendrites and dendritic branches.The Journal of biological chemistry · 2015Article
- Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion.Advances in experimental medicine and biology · 2015Review
- SH2B1 regulation of energy balance, body weight, and glucose metabolism.World journal of diabetes · 2014Review
- Phosphorylation of the adaptor protein SH2B1β regulates its ability to enhance growth hormone-dependent macrophage motility.Journal of cell science · 2013Article
- Tyrosyl phosphorylated PAK1 regulates breast cancer cell motility in response to prolactin through filamin A.Molecular endocrinology (Baltimore, Md.) · 2013Article
- Identification of SH2B1β as a focal adhesion protein that regulates focal adhesion size and number.Journal of cell science · 2011Article
- Adapter protein SH2B1beta binds filamin A to regulate prolactin-dependent cytoskeletal reorganization and cell motility.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Phosphorylation controls a dual-function polybasic nuclear localization sequence in the adapter protein SH2B1β to regulate its cellular function and distribution.Journal of cell science · 2011Article
- The glomerular podocyte as a target of growth hormone action: implications for the pathogenesis of diabetic nephropathy.Current diabetes reviews · 2011Review
- Diet-induced obesity in male mice is associated with reduced fertility and potentiation of acrylamide-induced reproductive toxicity.Biology of reproduction · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Src homology 2 (SH2) domain-containing adapter protein SH2B1beta plays a role in severe obesity, leptin and insulin resistance, and infertility. SH2B1beta was initially identified as a Janus tyrosine kinase 2 (JAK2) substrate, and it has been implicated in cell motility and regulation of the actin rearrangement in response to GH and platelet-derived growth factor. SH2B1beta is also required for maximal actin-based motility of Listeria. Here we have used a low-speed pelleting assay and electron microscopy to demonstrate that SH2B1beta has two actin-binding sites and that it cross-links actin filaments in vitro. Wild-type SH2B1beta localized to cell ruffles and along filopodia, but deletion of amino acids 150-200 (the first actin-binding site) led to mislocalization of the protein to filopodia tip complexes where it colocalized with vasodilator-stimulated phosphoprotein (VASP). Based on studies performed in VASP-deficient MVD7(-/-) cells, with or without green fluorescent protein-VASP reconstitution, we concluded that the proper intracellular localization of native SH2B1beta required the presence of the first SH2B1beta actin-binding site and VASP. Finally, we found that both SH2B1beta actin-binding domains were required for maximal GH- and prolactin-induced cell ruffling. Together, these results suggest that SH2B1beta functions as an adapter protein that cross-links actin filaments, leading to modulation of cellular responses in response to JAK2 activation.
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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.