scholarly journals Crystal Structure of the Epo1-Bem3 Complex for Bud Growth

2021 ◽  
Vol 22 (8) ◽  
pp. 3812
Author(s):  
Jin Wang ◽  
Lei Li ◽  
Zhenhua Ming ◽  
Lijie Wu ◽  
Liming Yan
Keyword(s):  
Crystal Structure ◽  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Protein Complex ◽  
Molecular Architecture ◽  
Hydrogen Deuterium ◽  
Bud Growth ◽  
Structural Insight ◽  
Guanosine Triphosphatase ◽  
Insight Into

Tubules of the endoplasmic reticulum (ER) spread into the buds of yeast by an actin-based mechanism and, upon entry, become attached to the polarisome, a proteinaceous micro-compartment below the tip of the bud. The minimal tether between polarisome and cortical ER is formed by a protein complex consisting of Epo1, a member of the polarisome, Scs2, a membrane protein of the ER and Cdc42 guanosine triphosphatase-activating protein Bem3. Here, we report the crystal structure of a complex between Epo1 and Bem3. In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1. Our findings provide a first structural insight into the molecular architecture of the link between cortical ER and the polarisome.

scholarly journals Bag6 complex contains a minimal tail-anchor–targeting module and a mock BAG domain

2014 ◽  
Vol 112 (1) ◽  
pp. 106-111 ◽  
Author(s):  
Jee-Young Mock ◽  
Justin William Chartron ◽  
Ma’ayan Zaslaver ◽  
Yue Xu ◽  
Yihong Ye ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Endoplasmic Reticulum ◽  
Complex Network ◽  
Binding Sites ◽  
Transmembrane Domain ◽  
Degradation Pathway ◽  
Tetratricopeptide Repeat ◽  
Endoplasmic Reticulum Associated Degradation ◽  
Structural Insight ◽  
Insight Into

BCL2-associated athanogene cochaperone 6 (Bag6) plays a central role in cellular homeostasis in a diverse array of processes and is part of the heterotrimeric Bag6 complex, which also includes ubiquitin-like 4A (Ubl4A) and transmembrane domain recognition complex 35 (TRC35). This complex recently has been shown to be important in the TRC pathway, the mislocalized protein degradation pathway, and the endoplasmic reticulum-associated degradation pathway. Here we define the architecture of the Bag6 complex, demonstrating that both TRC35 and Ubl4A have distinct C-terminal binding sites on Bag6 defining a minimal Bag6 complex. A crystal structure of the Bag6–Ubl4A dimer demonstrates that Bag6–BAG is not a canonical BAG domain, and this finding is substantiated biochemically. Remarkably, the minimal Bag6 complex defined here facilitates tail-anchored substrate transfer from small glutamine-rich tetratricopeptide repeat-containing protein α to TRC40. These findings provide structural insight into the complex network of proteins coordinated by Bag6.

scholarly journals Molecular architecture of the endocytic TPLATE complex

2021 ◽  
Vol 7 (9) ◽  
pp. eabe7999
Author(s):  
Klaas Yperman ◽  
Jie Wang ◽  
Dominique Eeckhout ◽  
Joanna Winkler ◽  
Lam Dai Vu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Structural Approach ◽  
Eukaryotic Cells ◽  
Molecular Architecture ◽  
Membrane Proteome ◽  
Complex Assembly ◽  
Membrane Interaction ◽  
Structural Insight ◽  
Fresh Insight ◽  
Insight Into

Eukaryotic cells rely on endocytosis to regulate their plasma membrane proteome and lipidome. Most eukaryotic groups, except fungi and animals, have retained the evolutionary ancient TSET complex as an endocytic regulator. Unlike other coatomer complexes, structural insight into TSET is lacking. Here, we reveal the molecular architecture of plant TSET [TPLATE complex (TPC)] using an integrative structural approach. We identify crucial roles for specific TSET subunits in complex assembly and membrane interaction. Our data therefore generate fresh insight into the differences between the hexameric TSET in Dictyostelium and the octameric TPC in plants. Structural elucidation of this ancient adaptor complex represents the missing piece in the coatomer puzzle and vastly advances our functional as well as evolutionary insight into the process of endocytosis.

Structural Insight Into Protein Binding of Boron Tracedrug UTX-97 Revealed by the Co-Crystal Structure With Lysozyme at 1.26 Å Resolution

2016 ◽  
Vol 105 (8) ◽  
pp. 2298-2301
Author(s):  
Yukio Morimoto ◽  
Hideko Nagasawa ◽  
Yoshihiro Uto ◽  
Toshiyuki Chatake ◽  
Hitoshi Hori
Keyword(s):  
Crystal Structure ◽  
Protein Binding ◽  
Structural Insight ◽  
Insight Into

Structural Insight into the Dioxygenation of Nitroarene Compounds: the Crystal Structure of Nitrobenzene Dioxygenase

2005 ◽  
Vol 348 (5) ◽  
pp. 1139-1151 ◽  
Author(s):  
Rosmarie Friemann ◽  
Maja M. Ivkovic-Jensen ◽  
Daniel J. Lessner ◽  
Chi-Li Yu ◽  
David T. Gibson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Structural Insight ◽  
Insight Into

scholarly journals A protein complex containing Epo1p anchors the cortical endoplasmic reticulum to the yeast bud tip

2014 ◽  
Vol 208 (1) ◽  
pp. 71-87 ◽  
Author(s):  
Joachim Neller ◽  
Alexander Dünkler ◽  
Reinhild Rösler ◽  
Nils Johnsson
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Direct Transfer ◽  
Directed Movement ◽  
Contact Sites ◽  
Specific Contact ◽  
Bud Growth ◽  
Guanosine Triphosphatase ◽  
Transfer Of Information ◽  
Cortical Endoplasmic Reticulum

The cortical endoplasmic reticulum (cER) of yeast underlies the plasma membrane (PM) at specific contact sites to enable a direct transfer of information and material between both organelles. During budding, directed movement of cER to the young bud followed by subsequent anchorage at its tip ensures the faithful inheritance of this organelle. The ER membrane protein Scs2p tethers the cER to the PM and to the bud tip through so far unknown receptors. We characterize Epo1p as a novel member of the polarisome that interacts with Scs2p exclusively at the cell tip during bud growth and show that Epo1p binds simultaneously to the Cdc42p guanosine triphosphatase–activating protein Bem3p. Deletion of EPO1 or deletion of BEM3 in a polarisome-deficient strain reduces the amount of cER at the tip. This analysis therefore identifies Epo1p as a novel and important component of the polarisome that promotes cER tethering at sites of polarized growth.

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