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Sharpin-Arp2/3 interaction promotes lamellipodium formation.
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The binding of SHARPIN or HOIL-1L facilitates the E2 loading of HOIP.
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SIPL1 contributes to promote resistance to tamoxifen in Breast cancer cells through both AKT and NF-kappaB actions.
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the present study found that loss of the NEMO-SHARPIN interaction impaired recruitment of truncated NEMO forms into punctuate structures that are transiently formed on cell stimulation and thus led to a defect in linear ubiquitination
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LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation.
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Overexpression of SHARPIN in Prostate cancer cells promoted cell growth and reduced apoptosis through NF-kB/ERK/Akt pathway and apoptosis-associated proteins. SHARPIN enhances the metastasis of prostate cancer and impair patient survivals.
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Our study firstly identifies the role of SHARPIN in promoting wild-type P53 degradation and correlates with poor prognosis in P53 wild-type breast cancer.
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Data show that SHANK-associated RH domain interacting protein (SHARPIN) gene expression in breast cancer patients predicts clinical outcomes.
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the roles of SHARPIN in inhibiting integrin activity and supporting linear ubiquitination are (molecularly) distinct.
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progesterone significantly reduced SIPL1 mRNA and protein expression in MCF7 cells. As progesterone enhances breast cancer tumorigenesis in context dependent manner, inhibition of SIPL1 expression may contribute to progesterone's non-tumorigenic function
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SIPL1 binds PTEN and enhances PTEN polyubiquitination.
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Sharpin deficiency sensitized primary murine keratinocytes, human keratinocytes, and mouse embryonic fibroblasts to TNF-induced apoptosis.
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SIPL1 promotes AKT activation by decreasing the amount of PTEN protein in CHO-K1 cells.
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SHARPIN controls lymphocyte migration by endogenously maintaining LFA-1 inactive to allow adjustable detachment of the uropods in polarized cells.
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crystals of SHARPIN belonged to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 61.55, c = 222.81 A
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the crystal structure of the N-terminal portion of SHARPIN, which adopts the highly conserved pleckstrin homology superfold that is often used as a scaffold to create protein interaction modules
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SHARPIN inhibits the critical switching of beta1-integrins from inactive to active conformations.
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SHARPIN is an additional component of LUBAC; SHARPIN-containing complexes can linearly ubiquitinate NEMO and activated NF-kappaB
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Data report the identification of the related proteins Sipl1 (Shank-interacting protein-like 1) and Rbck1 (RBCC protein interacting with PKC1) as novel interaction partners of Eya1.
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Suggest that Sharpin is not an inert scaffold protein, but may play tumor-associated roles during cancer biogenesis.
