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PubMed:18577513 JSONTXT 22 Projects

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Id Subject Object Predicate Lexical cue
T1 0-135 Sentence denotes The ubiquitin-protein ligase Nedd4-2 differentially interacts with and regulates members of the Tweety family of chloride ion channels.
T2 136-291 Sentence denotes The Tweety proteins comprise a family of chloride ion channels with three members identified in humans (TTYH1-3) and orthologues in fly and murine species.
T3 292-431 Sentence denotes In humans, increased TTYH2 expression is associated with cancer progression, whereas fly Tweety is associated with developmental processes.
T4 432-715 Sentence denotes Structurally, Tweety proteins are characterized by five membrane-spanning domains and N-glycan modifications important for trafficking to the plasma membrane, where these proteins are oriented with the amino terminus located extracellularly and the carboxyl terminus cytoplasmically.
T5 716-894 Sentence denotes In addition to N-glycosylation, ubiquitination mediated by the HECT type E3 ubiquitin ligase Nedd4-2 is a post-translation modification important in regulating membrane proteins.
T6 895-1067 Sentence denotes In the present study, we performed a comprehensive analysis of the ability of each of TTYH1-3 to interact with Nedd4-2 and to be ubiquitinated and regulated by this ligase.
T7 1068-1274 Sentence denotes Our data indicate that Nedd4-2 binds to two family members, TTYH2 and TTYH3, which contain consensus PY ((L/P)PXY) binding sites for HECT type E3 ubiquitin ligases, but not to TTYH1, which lacks this motif.
T8 1275-1332 Sentence denotes Consistently, Nedd4-2 ubiquitinates both TTYH2 and TTYH3.
T9 1333-1492 Sentence denotes Importantly, we have shown that endogenous TTYH2 and Nedd4-2 are binding partners and demonstrated that the TTYH2 PY motif is essential for these interactions.
T10 1493-1640 Sentence denotes We have also shown that Nedd4-2-mediated ubiquitination of TTYH2 is a critical regulator of cell surface and total cellular levels of this protein.
T11 1641-1831 Sentence denotes These data, indicating that Nedd4-2 differentially interacts with and regulates TTYH1-3, will be important for understanding mechanisms controlling Tweety proteins in physiology and disease.