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we demonstrated that HPIP silencing suppressed TGF-beta1 (show TGFB1 Proteins)-induced EMT (show ITK Proteins) in lung cancer cells by inhibiting Smad2 (show SMAD2 Proteins) activation.
our study demonstrated that knockdown of HPIP significantly inhibits the proliferation and migration/invasion of HNSCC cells by suppressing the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway.
these structural variations in CD2BP1 gene due to the mutations could be one of the strongest reasons to demonstrate the involvement of these gene variations in the patients with rheumatoid arthritis.
PSTPIP1 was found to interact with pyrin (show MEFV Proteins) at the leading edge during cell migration.
Molecular interactions between HPIP and FAK (show PTK2 Proteins), and HPIP and calpain2 regulate cell adhesion and migration through modulation of focal adhesion dynamics.
Case Report: missense mutation in PSTPIP1, the gene responsible for PAPA (show PAPPA Proteins) syndrome.
we have shown that PSTPIP1 regulates T-cell activation upon CD3 and CD28 stimulation, independently of CD2 costimulation. PSTPIP1 acts downstream of proximal TCR signaling, inhibiting several transcription factors.
PSTPIP1 has a role in the pathogenesis of pyoderma gangrenosum through filopodia formation resulting in extracellular matrix degradation
novel mutaations found in PSTPIP1 gene in patients with pyoderma gangrenosum
The CCTG (show CCT3 Proteins) repeat in the PSTPIP1 promoter may play a role in the pathogenesis of aseptic abscess syndrome and Crohn's disease.
analysis of inflammation in mice ectopically expressing human Pyogenic Arthritis, Pyoderma Gangrenosum, and Acne (PAPA (show PAPPA Proteins)) Syndrome-associated PSTPIP1 A230T mutant proteins
the intracellular Fas ligand (FasL (show FASL Proteins)) domain binding to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL (show FASL Proteins)
PSTPIP1 is a novel component of the leukocyte uropod that regulates endocytosis and cell migration
The protein encoded by this gene binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. The encoded protein appears to be a scaffold protein and a regulator of the actin cytoskeleton. It has also been shown to bind ABL1, PTPN18, WAS, CD2AP, and PTPN12. Mutations in this gene are a cause of PAPA syndrome.
proline-serine-threonine phosphatase interacting protein 1
, proline-serine-threonine phosphatase-interacting protein 1
, CD2 antigen-binding protein 1
, CD2 cytoplasmic tail-binding protein
, CD2-binding protein 1
, PEST phosphatase-interacting protein 1