{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T07:49:15Z","timestamp":1781077755509,"version":"3.54.1"},"reference-count":26,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2014,8,5]],"date-time":"2014-08-05T00:00:00Z","timestamp":1407196800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Fundaci\u00ef\u00bf\u00bdn Ram\u00ef\u00bf\u00bdn Areces"},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia e Innovaci\u00ef\u00bf\u00bdn","doi-asserted-by":"crossref","award":["SAF2009-09724"],"award-info":[{"award-number":["SAF2009-09724"]}],"id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2014,9]]},"abstract":"Proline\u2010serine\u2010threonine phosphatase interacting protein\u00a01 (PSTPIP<\/jats:styled-content>1) is an adaptor protein associated with the cytoskeleton that is mainly expressed in hematopoietic cells. Mutations in PSTPIP<\/jats:styled-content>1 cause the rare autoinflammatory disease called pyogenic arthritis, pyoderma gangrenosum, and acne. We carried out this study to further our knowledge on PSTPIP<\/jats:styled-content>1 function in T\u00a0cells, particularly in relation to the phosphatase lymphoid phosphatase (LYP<\/jats:styled-content>), which is involved in several autoimmune diseases. LYP<\/jats:styled-content>\u2013PSTPIP<\/jats:styled-content>1 binding occurs through the C\u2010terminal homology domain of LYP<\/jats:styled-content> and the F\u2010BAR<\/jats:styled-content> domain of PSTPIP<\/jats:styled-content>1. PSTPIP<\/jats:styled-content>1 inhibits T\u2010cell activation upon T\u2010cell receptor (TCR<\/jats:styled-content>) and CD<\/jats:styled-content>28 engagement, regardless of CD<\/jats:styled-content>2 costimulation. This function of PSTPIP<\/jats:styled-content>1 depends on the presence of an intact SH<\/jats:styled-content>3 domain rather than on the F\u2010BAR<\/jats:styled-content> domain, indicating that ligands of the F\u2010BAR<\/jats:styled-content> domain, such as the PEST<\/jats:styled-content> phosphatases LYP<\/jats:styled-content> and PTP<\/jats:styled-content>\u2010PEST<\/jats:styled-content>, are not critical for its negative regulatory role in TCR<\/jats:styled-content> signaling. Additionally, PSTPIP<\/jats:styled-content>1 mutations that cause the pyogenic arthritis, pyoderma gangrenosum and acne syndrome do not affect PSTPIP<\/jats:styled-content>1 function in T\u2010cell activation through the TCR<\/jats:styled-content>.<\/jats:p><\/jats:sec>Structured digital abstract<\/jats:title>\n\n\nLYP<\/jats:ext-link>\u00a0physically interacts<\/jats:ext-link>\u00a0with\u00a0PSTPIP1<\/jats:ext-link>\u00a0by\u00a0pull down<\/jats:ext-link>\u00a0(View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nPSTPIP1<\/jats:ext-link>\u00a0physically interacts<\/jats:ext-link>\u00a0with\u00a0LYP<\/jats:ext-link>\u00a0by\u00a0anti tag coimmunoprecipitation<\/jats:ext-link>\u00a0(1<\/jats:ext-link>,\u00a02<\/jats:ext-link>,\u00a03<\/jats:ext-link>,\u00a04<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nLYP<\/jats:ext-link>\u00a0physically interacts<\/jats:ext-link>\u00a0with\u00a0PSTPIP1<\/jats:ext-link>\u00a0by\u00a0anti bait coip<\/jats:ext-link>\u00a0(View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12912","type":"journal-article","created":{"date-parts":[[2014,7,5]],"date-time":"2014-07-05T06:07:49Z","timestamp":1404540469000},"page":"3844-3854","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Proline\u2010serine\u2010threonine phosphatase interacting protein\u00a01 inhibition of T\u2010cell receptor signaling depends on its SH<\/scp>3 domain"],"prefix":"10.1111","volume":"281","author":[{"given":"Tamara","family":"Marcos","sequence":"first","affiliation":[{"name":"Instituto de Biolog\u00eda y Gen\u00e9tica Molecular (IBGM) CSIC\u2010Universidad de Valladolid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Virginia","family":"Ruiz\u2010Mart\u00edn","sequence":"additional","affiliation":[{"name":"Instituto de Biolog\u00eda y Gen\u00e9tica Molecular (IBGM) CSIC\u2010Universidad de Valladolid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda Luisa","family":"de la Puerta","sequence":"additional","affiliation":[{"name":"Instituto de Biolog\u00eda y Gen\u00e9tica Molecular (IBGM) CSIC\u2010Universidad de Valladolid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio G.","family":"Trinidad","sequence":"additional","affiliation":[{"name":"Instituto de Biolog\u00eda y Gen\u00e9tica Molecular (IBGM) CSIC\u2010Universidad de Valladolid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mar\u00eda del Carmen","family":"Rodr\u00edguez","sequence":"additional","affiliation":[{"name":"Instituto de Biolog\u00eda y Gen\u00e9tica Molecular (IBGM) CSIC\u2010Universidad de Valladolid Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel Angel","family":"de la Fuente","sequence":"additional","affiliation":[{"name":"Instituto de Biolog\u00eda y 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