Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5
- Sangho Lee, Y. Tsai, J. Hurley
- Biology, ChemistryNature Structural &Molecular Biology
- 2006
The structure of the N-terminal portion of Rabex-5 bound to ubiquitin at 2.5-Å resolution shows that RabEx-5–ubiquitin interactions occur at two sites, including a new type of ubiquitIn-binding domain, an inverted ubiquit in-interacting motif, and a diaromatic patch on the A20 zinc finger, which binds with ∼22-μM affinity to a polar region centered on Asp58 of ubiqu
Signal-Mediated, AP-1/Clathrin-Dependent Sorting of Transmembrane Receptors to the Somatodendritic Domain of Hippocampal Neurons
- G. Farías, L. Cuitino, J. Bonifacino
- BiologyNeuron
- 6 September 2012
The human V3 pituitary vasopressin receptor: ligand binding profile and density-dependent signaling pathways.
- M. Thibonnier, J. Preston, N. Dulin, P. Wilkins, L. Berti-Mattera, R. Mattera
- Biology, MedicineEndocrinology
- 1 October 1997
The human V3R has a pharmacological profile clearly distinct from that of the human V1R and V2R and activates several signaling pathways via different G proteins, depending on the level of receptor expression.
Divalent interaction of the GGAs with the Rabaptin‐5–Rabex‐5 complex
- R. Mattera, C. Arighi, R. Lodge, M. Zerial, J. Bonifacino
- BiologyEMBO Journal
- 2 January 2003
It is demonstrated that the GGAs, a family of Arf‐dependent clathrin adaptors involved in selection of TGN cargo, interact with the Rabaptin‐5–Rabex‐5 complex, a Rab4/Rab5 effector regulating endosome fusion.
The Rab5 Guanine Nucleotide Exchange Factor Rabex-5 Binds Ubiquitin (Ub) and Functions as a Ub Ligase through an Atypical Ub-interacting Motif and a Zinc Finger Domain*
- R. Mattera, Y. Tsai, A. Weissman, J. Bonifacino
- Biology, ChemistryJournal of Biological Chemistry
- 10 March 2006
The identification of the 401-462 and 551-661 coiled-coils as the regions in Rabex-5 and Rabaptin-5, respectively, that interact with one another and the demonstration that RabEx-5 is a ubiquitIn ligase that binds ubiquitin and undergoes ubiquitination indicates that its role in endosome fusion may be subject to additional regulation by ubiquit in-dependent modifications.
Restricted Location of PSEN2/γ-Secretase Determines Substrate Specificity and Generates an Intracellular Aβ Pool
- R. Sannerud, C. Esselens, W. Annaert
- Biology, ChemistryCell
- 30 June 2016
The clathrin adaptor AP-1A mediates basolateral polarity.
- D. Gravotta, J. M. Carvajal-Gonzalez, E. Rodriguez-Boulan
- Biology, ChemistryDevelopmental Cell
- 17 April 2012
AP-4 mediates export of ATG9A from the trans-Golgi network to promote autophagosome formation
- R. Mattera, S. Park, Raffaella De Pace, Carlos M. A. Guardia, J. Bonifacino
- Biology, MedicineProceedings of the National Academy of Sciences…
- 27 November 2017
It is demonstrated that AP-4 sorts ATG9A, the only transmembrane component of the core autophagy machinery, from the trans-Golgi network to peripheral compartments, required to promote the early steps of autophagosome formation.
Molecular pharmacology of human vasopressin receptors.
- M. Thibonnier, D. M. Conarty, J. Preston, P. Wilkins, L. Berti-Mattera, R. Mattera
- Biology, MedicineAdvances in Experimental Medicine and Biology
- 1998
None of the 22 AVP/OT analogs tested has a better affinity for the human V3R than AVP itself, and several peptide antagonists do not select well between V1R and OTR, underscoring the need for developing specific and potent analogs interacting specifically with a given human A VP/OT receptor subtype.
Conservation and Diversification of Dileucine Signal Recognition by Adaptor Protein (AP) Complex Variants*
- R. Mattera, M. Boehm, Rittik Chaudhuri, Yogikala Prabhu, J. Bonifacino
- Biology, ChemistryJournal of Biological Chemistry
- 19 November 2010
The clathrin-associated, heterotetrameric adaptor protein (AP) complexes, AP-1, AP-2, and AP-3, recognize signals in the cytosolic domains of transmembrane proteins, leading to their sorting to…
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