Proline-serine-threonine phosphatase-interacting protein 1

Definition:

Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils.

References:

[1]. Andrea L Waite, et al. Pyrin Modulates the Intracellular Distribution of PSTPIP1. PLoS One. 2009 Jul 7;4(7):e6147. [Content Brief]

[2]. Andrea L Waite, et al. Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin. Exp Biol Med (Maywood). 2009 Jan;234(1):40-52. [Content Brief]

[3]. Je-Wook Yu, et al. Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants. Mol Cell. 2007 Oct 26;28(2):214-27. [Content Brief]

[4]. J Li, et al. A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. EMBO J. 1998 Dec 15;17(24):7320-36. [Content Brief]

[5]. Kate M Cooper, et al. The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration. Mol Biol Cell. 2008 Aug;19(8):3180-91. [Content Brief]

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