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Describe an autoinhibitory mechanism for ITCH ubiquitin ligase involving a linker-HECT domain interaction. This intramolecular interaction traps the HECT enzyme in its inactive state and can be relieved by linker phosphorylation.
Data show that the E3 ubiquitin ligase (show MUL1 Proteins) Itch forms a complex with tricellulin (show MARVELD2 Proteins) and thereby enhances its ubiquitination.
ASPP2 (show TP53BP2 Proteins) suppresses invasion, peritoneal dissemination and TGF-beta1 (show TGFB1 Proteins)-induced EMT (show ITK Proteins) by inhibiting Smad7 (show SMAD7 Proteins) degradation mediated by ITCH in gastric cancer cells.
WBP2 (show WBP2 Proteins)/ITCH signaling functions to link the intricate Wnt (show WNT2 Proteins) and Hippo signaling networks in breast cancer.
The cellular ubiquitin ligase, Itch, is required for Kaposi's sarcoma herpesvirus RTA (show RBM9 Proteins) induced degradation of vFLIP.
Results indicate that TAX1BP1 (show TAX1BP1 Proteins) functions as an adaptor molecule for Itch to target MAVS (show MAVS Proteins) during RNA virus infection and thus restrict virus-induced apoptosis.
These data demonstrate that Itch, ubiquitin, and Alix (show PDCD6IP Proteins) control the BFRF1-mediated modulation of the nuclear envelope and human herpesvirus 4 maturation, uncovering novel regulatory mechanisms of nuclear egress of viral nucleocapsids.
The authors demonstrate that the PPxY L domain motif of ebolavirus VP40 interacts specifically with the WW domain of the host E3 ubiquitin ligase (show MUL1 Proteins) ITCH.
Molecular basis of interactions between SH3 domain-containing proteins and the proline-rich region of the ubiquitin ligase Itch.
cir (show KCNJ5 Proteins)-ITCH may play an inhibitory role in lung cancer progression by enhancing its parental gene, ITCH, expression
this study identified a previously unknown role for Itch in regulating IL-17 (show IL17A Proteins)-mediated colonic inflammation and carcinogenesis
Itch monoubiquitinates SMN (show STMN1 Proteins) and monoubiquitination of SMN (show STMN1 Proteins) plays an important role in regulating its cellular localization.
ITCH targets TXNIP (show TXNIP Proteins) for ubiquitin-proteasome degradation in cardiomyocytes and ameliorates reactive oxygen species-induced cardiotoxicity through the thioredoxin (show TXN Proteins) system.
CUL4B links two distinct spermatogenetic processes to a single E3 ligase, highlighting the significance of ubiquitin modification during spermatogenesis.
Impaired ITCH results in heightened TNF (show TNF Proteins) signaling. ITCH-/- mouse's spontaneous lung inflammation and subsequent death can be delayed when TNF (show TNF Proteins) signaling is genetically deleted.
ITCH modulates SIRT6 (show SIRT6 Proteins) and SREBP2 (show SREBF2 Proteins) to influence lipid metabolism and atherosclerosis in ApoE (show APOE Proteins) null mice
In the absence of Ndfip1, the Nedd4 family member Itch can bind an E2 but cannot accept ubiquitin onto its catalytic cysteine.
The E3 ubiquitin ligase (show MUL1 Proteins) Itch inhibits p38alpha (show MAPK14 Proteins) signaling and skin inflammation through the ubiquitylation of Tab1 (show TAB1 Proteins).
Ndfip1 (show NDFIP1 Proteins) regulates itch ligase activity and airway inflammation via UbcH7 (show UBE2L3 Proteins).
The expression of Th2 cytokines by Treg cells was increased in the absence of Itch. Fate mapping revealed that a fraction of Treg cells lost Foxp3 (show FOXP3 Proteins) expression independently of Itch.
This gene encodes a member of the Nedd4 family of HECT domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein substrates, thus targeting specific proteins for lysosomal degradation. The encoded protein plays a role in multiple cellular processes including erythroid and lymphoid cell differentiation and the regulation of immune responses. Mutations in this gene are a cause of syndromic multisystem autoimmune disease. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
E3 ubiquitin-protein ligase Itchy homolog
, NFE2-associated polypeptide 1
, atrophin-1 interacting protein 4
, dJ468O1.1 (atrophin 1 interacting protein 4 (AIP4))
, itchy E3 ubiquitin protein ligase homolog
, E3 ubiquitin-protein ligase Itchy