RT info:eu-repo/semantics/article
T1 Proline‐serine‐threonine phosphatase interacting protein 1 inhibition of T‐cell receptor signaling depends on its SH3 domain
A1 Marcos, Tamara
A1 Ruiz Martín, Virginia
A1 Puerta Turrillas, María Luisa de la
A1 García Trinidad, Antonio
A1 García Rodríguez, María Del Carmen
A1 Fuente García, Miguel Ángel de la
A1 Sánchez Crespo, Mariano
A1 Alonso García, Andrés
A1 Bayón Prieto, Yolanda
K1 Biomedicina
K1 PTPN22
K1 T-cell receptor
K1 T cell
K1 proline-serine-threonine phosphatase interacting protein 1 (PSTPIP1)
K1 pyogenic arthritis, pyoderma gangrenosum and acne (PAPA)
K1 24 Ciencias de la Vida
AB Proline-serine-threonine phosphatase interacting protein 1 (PSTPIP1) is an adaptor protein associated with the cytoskeleton that is mainly expressed in hematopoietic cells. Mutations in PSTPIP1 cause the rare autoinflammatory disease called pyogenic arthritis, pyoderma gangrenosum, and acne. We carried out this study to further our knowledge on PSTPIP1 function in T cells, particularly in relation to the phosphatase lymphoid phosphatase (LYP), which is involved in several autoimmune diseases. LYP-PSTPIP1 binding occurs through the C-terminal homology domain of LYP and the F-BAR domain of PSTPIP1. PSTPIP1 inhibits T-cell activation upon T-cell receptor (TCR) and CD28 engagement, regardless of CD2 costimulation. This function of PSTPIP1 depends on the presence of an intact SH3 domain rather than on the F-BAR domain, indicating that ligands of the F-BAR domain, such as the PEST phosphatases LYP and PTP-PEST, are not critical for its negative regulatory role in TCR signaling. Additionally, PSTPIP1 mutations that cause the pyogenic arthritis, pyoderma gangrenosum and acne syndrome do not affect PSTPIP1 function in T-cell activation through the TCR.
PB Wiley
SN 1742-464X
YR 2014
FD 2014-09
LK https://uvadoc.uva.es/handle/10324/73134
UL https://uvadoc.uva.es/handle/10324/73134
LA eng
NO The FEBS Journal, 2014, vol. 281, n. 17, p. 3844-3854
NO Producción Científica
DS UVaDOC
RD 05-abr-2025