TRIM32 Proteine (TRIM32)

Human Tripartite Motif Containing 32 (TRIM32) Interaktionspartner

1. TRIM32 as a crucial positive regulator of Herpes Simplex Virus type 1 (HSV-1) induced IFN-beta (zeige IFNB1 Proteine) production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea.

2. HSP70 (zeige HSP70 Proteine)-TRIM32 complex is biochemically distinct from the previously characterized 14-3-3 (zeige YWHAQ Proteine)-TRIM32 phospho-complex.

3. Data suggest that, in cardiomyocytes, TRIM32 attenuates activation of SRF signaling and hypertrophy due to dysbindin; TRIM24 promotes these effects. TRIM32 promotes dysbindin degradation; TRIM24 protects dysbindin from degradation. (TRIM = tripartite motif-containing protein; SRF = serum response factor)

4. Duchenne muscular dystrophy (zeige DMD Proteine) muscles showed a selective up-regulation of the ubiquitin ligase tripartite motif-containing protein 32 (TRIM32). The induction of TRIM32 was due to a transcriptional effect and it correlated with disease severity.

5. we provide a detailed characterization of the TRIM (zeige TRAT1 Proteine) ligases TRIM25 (zeige TRIM25 Proteine) and TRIM32 and show how their oligomeric state is linked to catalytic activity

6. that TRIM32 plays a protective role in aortic banding-induced pathological cardiac remodelling by blocking Akt (zeige AKT1 Proteine)-dependent signalling

7. these findings suggest that TRIM32 might play important roles in the hepatocarcinogenesis.

8. results show a novel molecular cascade involving miR (zeige MLXIP Proteine)-155 and TRIM32 leading to HIV-1 Tat (zeige TAT Proteine)-induced attenuated proliferation of neural precursor cells; study also uncovered an unidentified role for miR (zeige MLXIP Proteine)-155 in modulating human neural stem cell proliferation, helping in better understanding of neural precursor cells and diseased brain

9. Studies indicate most-studied TRIpartite Motif (TRIM (zeige TRAT1 Proteine))-NHL proteins TRIM2 (zeige TRIM2 Proteine), TRIM3 (zeige TRIM3 Proteine), TRIM32 and TRIM71 (zeige TRIM71 Proteine), and their mutations have been linked to diseases.

10. Results suggest that Salmonella effector SseK3 binding to host tripartite motif-containing 32 protein (TRIM32) in the inhibition of nuclear factor kappa B (NF-kappaB (zeige NFKB1 Proteine)) activation: [SseK3]

Mouse (Murine) Tripartite Motif Containing 32 (TRIM32) Interaktionspartner

1. suppression of Trim32 promotes the recovery of neurological function after traumatic brain injury.

2. the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32.

3. TRIM32 is a novel essential positive factor modulating axonal regeneration and the recovery of motor function following SCI, possibly through suppressing proliferation of glial cells.

4. TRIM32 as a crucial positive regulator of Herpes Simplex Virus type 1 (HSV-1) induced IFN-beta (zeige IFNB1 Proteine) production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea.

5. TRIM32 protein expression is defective in atopic dermatitis lesional skin.

6. that TRIM32 plays a protective role in aortic banding-induced pathological cardiac remodelling by blocking Akt (zeige AKT1 Proteine)-dependent signalling

7. In summary, the data presented here reveal that TRIM32 directly regulates at least two of the four Yamanaka Factors (cMyc (zeige MYC Proteine) and Oct4 (zeige POU5F1 Proteine)), to modulate cell fate transitions.

8. TRIM32 represents a model of intrinsic immunity, in which a host protein directly senses and counters viral infection in a species specific fashion by directly limiting viral replication

9. NDRG2 (zeige NDRG2 Proteine) accumulated in skeletal muscle and myoblasts in the absence of TRIM32. NDRG2 (zeige NDRG2 Proteine) overexpression in myoblasts led to reduced cell proliferation and delayed cell cycle withdrawal during differentiation.

10. TRIM32 overexpression promotes cell oncogenic transformation and tumorigenesis in mice in a largely p53 (zeige TP53 Proteine)-dependent manner.