{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T07:38:36Z","timestamp":1770968316464,"version":"3.50.1"},"reference-count":92,"publisher":"The Endocrine Society","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Prolactin (PRL) regulates cytoskeletal rearrangement and cell motility. PRL-activated Janus tyrosine kinase 2 (JAK2) phosphorylates the p21-activated serine-threonine kinase (PAK)1 and the Src homology 2 (SH2) domain-containing adapter protein SH2B1\u03b2. SH2B1\u03b2 is an actin-binding protein that cross-links actin filaments, whereas PAK1 regulates the actin cytoskeleton by different mechanisms, including direct phosphorylation of the actin-binding protein filamin A (FLNa). Here, we have used a FLNa-deficient human melanoma cell line (M2) and its derivative line (A7) that stably expresses FLNa to demonstrate that SH2B1\u03b2 and FLNa are required for maximal PRL-dependent cell ruffling. We have found that in addition to two actin-binding domains, SH2B1\u03b2 has a FLNa-binding domain (amino acids 200\u2013260) that binds directly to repeats 17\u201323 of FLNa. The SH2B1\u03b2-FLNa interaction participates in PRL-dependent actin rearrangement. We also show that phosphorylation of the three tyrosines of PAK1 by JAK2, as well as the presence of FLNa, play a role in PRL-dependent cell ruffling. Finally, we show that the actin- and FLNa-binding-deficient mutant of SH2B1\u03b2 (SH2B1\u03b2 3\u0394) abolished PRL-dependent ruffling and PRL-dependent cell migration when expressed along with PAK1 Y3F (JAK2 tyrosyl-phosphorylation-deficient mutant). Together, these data provide insight into a novel mechanism of PRL-stimulated regulation of the actin cytoskeleton and cell motility via JAK2 signaling through FLNa, PAK1, and SH2B1\u03b2. We propose a model for PRL-dependent regulation of the actin cytoskeleton that integrates our findings with previous studies.<\/jats:p>","DOI":"10.1210\/me.2011-0056","type":"journal-article","created":{"date-parts":[[2011,5,14]],"date-time":"2011-05-14T00:14:10Z","timestamp":1305332050000},"page":"1231-1243","source":"Crossref","is-referenced-by-count":21,"title":["Adapter Protein SH2B1\u03b2 Binds Filamin A to Regulate Prolactin-Dependent Cytoskeletal Reorganization and Cell Motility"],"prefix":"10.1210","volume":"25","author":[{"given":"Leah","family":"Rider","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, University of Toledo, Toledo, Ohio 43606-3390"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria","family":"Diakonova","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Toledo, Toledo, Ohio 43606-3390"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"80","reference":[{"key":"2020071613390677400_B1","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1210\/edrv.19.3.0334","article-title":"Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice.","volume":"19","author":"Bole-Feysot","year":"1998","journal-title":"Endocr Rev"},{"key":"2020071613390677400_B2","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1023\/A:1018708704335","article-title":"Prolactin and mammary gland development.","volume":"4","author":"Horseman","year":"1999","journal-title":"J Mammary Gland Biol Neoplasia"},{"key":"2020071613390677400_B3","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1210\/er.2004-0016","article-title":"Development and potential clinical uses of human prolactin receptor antagonists.","volume":"26","author":"Goffin","year":"2005","journal-title":"Endocr Rev"},{"key":"2020071613390677400_B4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1677\/JOE-10-0069","article-title":"New concepts in prolactin biology.","volume":"206","author":"Bernichtein","year":"2010","journal-title":"J Endocrinol"},{"key":"2020071613390677400_B5","first-page":"695","article-title":"Expression of prolactin and prolactin receptor in human breast carcinoma. 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Genetic regulation of human breast carcinoma metastasis.","volume":"2","author":"Welch","year":"2000","journal-title":"Breast Cancer Res"},{"key":"2020071613390677400_B9","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1210\/er.2001-0036","article-title":"The role of prolactin in mammary carcinoma.","volume":"24","author":"Clevenger","year":"2003","journal-title":"Endocr Rev"},{"key":"2020071613390677400_B10","doi-asserted-by":"crossref","first-page":"75","DOI":"10.3233\/BD-2003-18108","article-title":"Role of prolactin\/prolactin receptor signaling in human breast cancer.","volume":"18","author":"Clevenger","year":"2003","journal-title":"Breast Dis"},{"key":"2020071613390677400_B11","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1177\/0269881107082624","article-title":"Adverse effects of prolactin in rodents and humans: breast and prostate cancer.","volume":"22","author":"Harvey","year":"2008","journal-title":"J 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