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Title: TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Authors:
;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OTHER
OSTI Identifier:
1322365
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America; Journal Volume: 113; Journal Issue: 36
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Ma, Wenfu, and Goldberg, Jonathan. TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. United States: N. p., 2016. Web. doi:10.1073/pnas.1605916113.
Ma, Wenfu, & Goldberg, Jonathan. TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. United States. doi:10.1073/pnas.1605916113.
Ma, Wenfu, and Goldberg, Jonathan. 2016. "TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats". United States. doi:10.1073/pnas.1605916113.
@article{osti_1322365,
title = {TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats},
author = {Ma, Wenfu and Goldberg, Jonathan},
abstractNote = {},
doi = {10.1073/pnas.1605916113},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 36,
volume = 113,
place = {United States},
year = 2016,
month = 8
}
  • Ancestral coatomer element 1 (ACE1) proteins assemble latticework coats for COPII vesicles and the nuclear pore complex. The ACE1 protein Sec31 and Sec13 make a 2:2 tetramer that forms the edge element of the COPII outer coat. In this study, we report that the COPII accessory protein Sec16 also contains an ACE1. The 165-kD crystal structure of the central domain of Sec16 in complex with Sec13 was solved at 2.7-Å resolution. Sec16 and Sec13 also make a 2:2 tetramer, another edge element for the COPII system. Domain swapping at the ACE1-ACE1 interface is observed both in the prior structure ofmore » Sec13-Sec31 and in Sec13-Sec16. A Sec31 mutant in which domain swapping is prevented adopts an unprecedented laminated structure, solved at 2.8-Å resolution. Our in vivo data suggest that the ACE1 element of Sec31 can functionally replace the ACE1 element of Sec16. Our data support Sec16 as a scaffold for the COPII system and a template for the Sec13-Sec31 coat.« less
  • COPI-coated vesicles form at the Golgi apparatus from two cytosolic components, ARF G protein and coatomer, a heptameric complex that can polymerize into a cage to deform the membrane into a bud. Although coatomer shares a common evolutionary origin with COPII and clathrin vesicle coat proteins, the architectural relationship among the three cages is unclear. Strikingly, the {alpha}{beta}-COP core of coatomer crystallizes as a triskelion in which three copies of a {beta}-COP {beta}-propeller domain converge through their axial ends. We infer that the trimer constitutes the vertex of the COPI cage. Our model proposes that the COPI cage is intermediatemore » in design between COPII and clathrin: COPI shares with clathrin an arrangement of three curved {alpha}-solenoid legs radiating from a common center, and COPI shares with COPII highly similar vertex interactions involving the axial ends of {beta}-propeller domains.« less
  • Solution processable semiconducting polymers have been under intense investigations due to their diverse applications from printed electronics to biomedical devices. However, controlling the macromolecular assembly across length scales during solution coating remains a key challenge, largely due to the disparity in timescales of polymer assembly and high-throughput printing/coating. Herein we propose the concept of dynamic templating to expedite polymer nucleation and the ensuing assembly process, inspired by biomineralization templates capable of surface reconfiguration. Molecular dynamic simulations reveal that surface reconfigurability is key to promoting template–polymer interactions, thereby lowering polymer nucleation barrier. Employing ionic-liquid-based dynamic template during meniscus-guided coating results inmore » highly aligned, highly crystalline donor-acceptor polymer thin films over large area (41cm 2) and promoted charge transport along both the polymer backbone and the π-π stacking direction in field-effect transistors. We further demonstrate that the charge transport anisotropy can be reversed by tuning the degree of polymer backbone alignment.« less
  • Sorting of endocytosed EGF receptor (EGFR) to internal vesicles of multivesicular bodies (MVBs) depends on sustained activation and ubiquitination of the EGFR. Ubiquitination of EGFR is mediated by the ubiquitin ligase Cbl, being recruited to the EGFR both directly and indirectly through association with Grb2. Endosomal sorting of ubiquitinated proteins further depends on interaction with ubiquitin binding adaptors like Hrs. Hrs localizes to flat, clathrin-coated domains on the limiting membrane of endosomes. In the present study, we have investigated the localization of EGFR, Cbl and Grb2 with respect to coated and non-coated domains of the endosomal membrane and to vesiclesmore » within MVBs. Both EGFR, Grb2, and Cbl were concentrated in coated domains of the limiting membrane before translocation to inner vesicles of MVBs. While almost all Hrs was in clathrin-positive coats, EGFR and Grb2 in coated domains only partially colocalized with Hrs and clathrin. The extent of colocalization of EGFR and Grb2 with Hrs and clathrin varied with time of incubation with EGF. These results demonstrate that both clathrin-positive and clathrin-negative electron dense coats exist on endosomes and are involved in endosomal sorting of the EGFR.« less