anti-SHANK-Associated RH Domain Interacting Protein (SHARPIN) Anticorps

Mouse (Murine) SHANK-Associated RH Domain Interacting Protein (SHARPIN) interaction partners

1. LUBAC-tethering motifs (LTMs) located N terminally to the UBL domains of HOIL-1L and SHARPIN heterodimerize and fold into a single globular domain.

2. Data show that keratinocyte-specific deletion of ubiquitin-protein ligases HOIP, HOIL-1 (E-KO) and shank-interacting protein-like 1 protein (SHARPIN) results in severe dermatitis causing postnatal lethality.

3. Both Sharpin/Fas and Sharpin/Fasl compound mutant mice developed an auto-inflammatory phenotype similar to that seen in Sharpin null mice, indicating that initiation of apoptosis by FAS signalling is likely not involved in the pathogenesis of this disease.

4. 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, highlighting the importance of specific targeted therapies in the IL-1 signaling blockade.

5. Itgb1 inhibition alleviates the chronic hyperproliferative dermatitis phenotype of Sharpin-deficient mice.

6. LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation.

7. Suppression of SHARPIN impaired cell proliferation, angiogenesis, and invasion and reduced levels of MMP-9 in Prostate cancer cells and reduced the size of Metastatic Lung tumors induced by these cells in mice.

8. 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.

9. Study found that the NZF domain of SHARPIN, but not that of HOIL-1L, is critical for effective protection from programmed cell death by enhancing the recruitment of the linear ubiquitin chain assembly complex to the activated TNFR complex. The binding activity to K63-linked ubiquitin chains that the NZF domain of SHARPIN, but not that of HOIL-1L, possesses appears to be involved in the recruitment.

10. this study reveals a critical function of SHARPIN in TCR-induced NF-kappaB and JNK signalling and thymic Treg cell generation

11. SHARPIN-deficient mice develop a chronic proliferative dermatitis presenting angiogenesis and lymphatic dilatation.

12. Study identifies a role for SHARPIN in TCR signaling whereby it maintains immunological homeostasis and tolerance by regulating Treg cells.

13. severity of the esophagitis was not affected by crossing SHARPIN-deficient mice with lymphocyte-deficient Rag1 null mice

14. Sharpin Controls Osteogenic Differentiation of Mesenchymal Bone Marrow Cells.

15. Data indicate that genetic ablation of caspase-1 and -11 from cpdm mice significantly reduced skin inflammation in sharpin-deficient mice.

16. Our results suggest that SHARPIN plays a significant role in skeletal homeostasis and that this role is strongly regulated through TNF pathways.

17. Sharpin deficiency sensitized primary murine keratinocytes, human keratinocytes, and mouse embryonic fibroblasts to TNF-induced apoptosis.

18. Tnfr1, but not Tnfr2, deficiency suppresses inflammation in sharpin deficient mice.

19. SHARPIN is required for optimal NLRP3 inflammasome activation.

20. Sharpin deficiency results in chronic proliferative dermatitis/ autoinflammatory disease in the absence of B and T lymphocytes and IL4/IL13 signaling.

Human SHANK-Associated RH Domain Interacting Protein (SHARPIN) interaction partners

1. Sharpin has a primary role during development of atopic dermatitis; it induces elevated expression of IL-33 and its orphan receptor ST2, FLG and STAT3 and NF-kappaB inactivation in HaCaT keratinocytes

2. identified a LUBAC-independent role for SHARPIN in enhancing PRMT5 activity that contributes to melanomagenesis through the SKI/SOX10 regulatory axis.

3. SHARPIN functions in the human megakaryocyte/platelet lineage through protein interactions at the nexus of integrin and immune/inflammatory signaling.

4. Sharpin-Arp2/3 interaction promotes lamellipodium formation.

5. The binding of SHARPIN or HOIL-1L facilitates the E2 loading of HOIP.

6. SIPL1 contributes to promote resistance to tamoxifen in Breast cancer cells through both AKT and NF-kappaB actions.

7. 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

8. LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation.

9. 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.

10. 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.

11. Data show that SHANK-associated RH domain interacting protein (SHARPIN) gene expression in breast cancer patients predicts clinical outcomes.

12. the roles of SHARPIN in inhibiting integrin activity and supporting linear ubiquitination are (molecularly) distinct.

13. 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

14. SIPL1 binds PTEN and enhances PTEN polyubiquitination.

15. Sharpin deficiency sensitized primary murine keratinocytes, human keratinocytes, and mouse embryonic fibroblasts to TNF-induced apoptosis.

16. SIPL1 promotes AKT activation by decreasing the amount of PTEN protein in CHO-K1 cells.

17. SHARPIN controls lymphocyte migration by endogenously maintaining LFA-1 inactive to allow adjustable detachment of the uropods in polarized cells.

18. 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

19. 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

20. SHARPIN inhibits the critical switching of beta1-integrins from inactive to active conformations.