Journal
FRONTIERS IN IMMUNOLOGY
Volume 12, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2021.585412
Keywords
proline-serine-threonine-phosphatase-interacting protein 2; autoinflammatory diseases; macrophages; osteoclast; PEST-PTPs
Categories
Funding
- National Natural Science Foundation of China [81770609]
- Anhui Medical University of Science and Technology [1704a0802161]
- University Synergy Innovation Program of Anhui Province [GXXT-2019-045]
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PSTPIP2, a member of the F-BAR domain family, plays important roles in immune and inflammatory processes, making it a potential therapeutic target for AIDs. While it has been found that proteins like PTP-PEST, SHIP1, and CSK can bind to PSTPIP2 and inhibit AIDs development, the exact mechanisms of PSTPIP2's function remain to be fully elucidated.
Proline-serine-threonine-phosphatase-interacting protein 2 (PSTPIP2) belongs to the Fes/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain family. It exhibits lipid-binding, membrane deformation, and F-actin binding activity, suggesting broader roles at the membrane-cytoskeleton interface. PSTPIP2 is known to participate in macrophage activation, neutrophil migration, cytokine production, and osteoclast differentiation. In recent years, it has been observed to play important roles in innate immune diseases and autoinflammatory diseases (AIDs). Current research indicates that the protein tyrosine phosphatase PTP-PEST, Src homology domain-containing inositol 5'-phosphatase 1 (SHIP1), and C-terminal Src kinase (CSK) can bind to PSTPIP2 and inhibit the development of AIDs. However, the mechanisms underlying the function of PSTPIP2 have not been fully elucidated. This article reviews the research progress and mechanisms of PSTPIP2 in AIDs. PSTPIP2 also provides a new therapeutic target for the treatment of AIDs.
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