{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T03:47:11Z","timestamp":1790048831941,"version":"4.0.1"},"reference-count":36,"publisher":"National Academy of Sciences","issue":"45","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2006,11,7]]},"abstract":"<jats:p>\n                    RGS-PX1 (also known as sorting nexin 13) is a member of both the regulator of G protein signaling (RGS) and sorting nexin (SNX) protein families. Biochemical and cell culture studies have shown that RGS-PX1\/SNX13 attenuates G\u03b1s-mediated signaling through its RGS domain and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. To understand the functions of RGS-PX1\/SNX13\n                    <jats:italic>in vivo<\/jats:italic>\n                    , we generated mice carrying targeted mutations of\n                    <jats:italic>Snx13<\/jats:italic>\n                    and found that systemic\n                    <jats:italic>Snx13<\/jats:italic>\n                    -null mice were embryonic lethal around midgestation.\n                    <jats:italic>Snx13<\/jats:italic>\n                    -null embryos had significant overall growth retardation and defects in neural tube closure, blood vessel formation, and the formation of the placental labyrinthine layer. Moreover, the\n                    <jats:italic>Snx13<\/jats:italic>\n                    -null visceral yolk sac endoderm cells showed dramatic changes in the organization of endocytic compartments, abundant autophagic vacuoles, and abnormal localization of several endocytic markers, including megalin, a receptor for nutrients and proteins; ARH, a coat protein that binds megalin; LAMP2; and LC3. These changes suggest that\n                    <jats:italic>Snx13<\/jats:italic>\n                    -null embryos are defective in nutrient uptake and transport, which may contribute to the other developmental abnormalities observed. Taken together, our findings demonstrate an essential role for RGS-PX1\/SNX13 in mouse development and provide previously undescribed insights into its cellular function in the regulation of endocytosis dynamics.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0607974103","type":"journal-article","created":{"date-parts":[[2006,11,2]],"date-time":"2006-11-02T08:25:30Z","timestamp":1162455930000},"page":"16776-16781","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":57,"title":["Essential role of RGS-PX1\/sorting nexin 13 in mouse development and regulation of endocytosis dynamics"],"prefix":"10.1073","volume":"103","author":[{"given":"Bin","family":"Zheng","sequence":"first","affiliation":[{"name":"Departments of *Cellular and Molecular Medicine and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tingdong","family":"Tang","sequence":"additional","affiliation":[{"name":"Departments of *Cellular and Molecular 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