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directly interacts with the ankyrin repeats of Shank; may be involved in regulating the function of Shank.
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results altogether demonstrate distinct roles of SHARPIN in initiating systemic inflammation and dermatitis. Furthermore, skin inflammation in Sharpin(cpdm) mice is specifically modulated by IL-1beta (Montrer IL1B Anticorps), highlighting the importance of specific targeted therapies in the IL-1 (Montrer IL1A Anticorps) signaling blockade.
Itgb1 (Montrer ITGB1 Anticorps) inhibition alleviates the chronic hyperproliferative dermatitis phenotype of Sharpin-deficient mice.
LUBAC components control TLR3 (Montrer TLR3 Anticorps)-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation.
Suppression of SHARPIN impaired cell proliferation, angiogenesis, and invasion and reduced levels of MMP-9 in P (Montrer EPHB2 Anticorps)rost (Montrer AKT1 Anticorps)ate cancer cells and reduced the size of Metastatic Lung tumors induced by these cells in mice.
Together, these data imply that SHARPIN regulates the normal invasive mammary gland branching morphogenesis in an epithelial cell extrinsic manner by controlling the organisation of the stromal extracellular matrix.
Study found that the NZF (Montrer PHF20 Anticorps) domain of SHARPIN, but not that of HOIL-1L (Montrer RBCK1 Anticorps), is critical for effective protection from programmed cell death by enhancing the recruitment of the linear ubiquitin chain assembly complex to the activated TNFR (Montrer TNFRSF1A Anticorps) complex. The binding activity to K63-linked ubiquitin chains that the NZF (Montrer PHF20 Anticorps) domain of SHARPIN, but not that of HOIL-1L (Montrer RBCK1 Anticorps), possesses appears to be involved in the recruitment.
this study reveals a critical function of SHARPIN in TCR-induced NF-kappaB (Montrer NFKB1 Anticorps) and JNK (Montrer MAPK8 Anticorps) signalling and thymic Treg cell generation
SHARPIN-deficient mice develop a chronic proliferative dermatitis presenting angiogenesis and lymphatic dilatation.
Study identifies a role for SHARPIN in TCR signaling whereby it maintains immunological homeostasis and tolerance by regulating Treg cells.
severity of the esophagitis was not affected by crossing SHARPIN-deficient mice with lymphocyte-deficient Rag1 (Montrer RAG1 Anticorps) null mice
Sharpin-Arp2 (Montrer ACTR2 Anticorps)/3 interaction promotes lamellipodium formation.
The binding of SHARPIN or HOIL-1L (Montrer RBCK1 Anticorps) facilitates the E2 loading of HOIP (Montrer RNF31 Anticorps).
SIPL1 contributes to promote resistance to tamoxifen in Breast cancer cells through both AKT (Montrer AKT1 Anticorps) and NF-kappaB (Montrer NFKB1 Anticorps) actions.
the present study found that loss of the NEMO (Montrer IKBKG Anticorps)-SHARPIN interaction impaired recruitment of truncated NEMO (Montrer IKBKG Anticorps) forms into punctuate structures that are transiently formed on cell stimulation and thus led to a defect in linear ubiquitination
Overexpression of SHARPIN in Prostate cancer cells promoted cell growth and reduced apoptosis through NF-kB/ERK (Montrer EPHB2 Anticorps)/Akt (Montrer AKT1 Anticorps) pathway and apoptosis-associated proteins. SHARPIN enhances the metastasis of prostate cancer and impair patient survivals.
Our study firstly identifies the role of SHARPIN in promoting wild-type P53 (Montrer TP53 Anticorps) degradation and correlates with poor prognosis in P53 (Montrer TP53 Anticorps) wild-type breast cancer.
Data show that SHANK-associated RH domain interacting protein (SHARPIN) gene expression in breast cancer patients predicts clinical outcomes.
the roles of SHARPIN in inhibiting integrin activity and supporting linear ubiquitination are (molecularly) distinct.
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
directly interacts with the ankyrin repeats of Shank; may be involved in regulating the function of Shank
, protein kinase C-interacting protein RBCC like 1
, shank-associated RH domain-interacting protein
, shank-interacting protein-like 1
, SHANK-associated RH domain interacting protein
, shank-interacting protein