scholarly journals Faculty Opinions recommendation of The ER membrane protein complex is a transmembrane domain insertase.

2019 ◽  
Author(s):  
Koreaki Ito
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Transmembrane Domain ◽  
Membrane Protein Complex ◽  
Er Membrane

scholarly journals The ER membrane protein complex is a transmembrane domain insertase

Science ◽  
2017 ◽  
Vol 359 (6374) ◽  
pp. 470-473 ◽  
Author(s):  
Alina Guna ◽  
Norbert Volkmar ◽  
John C. Christianson ◽  
Ramanujan S. Hegde
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Transmembrane Domain ◽  
Membrane Protein Complex ◽  
Er Membrane

scholarly journals The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Matthew J Shurtleff ◽  
Daniel N Itzhak ◽  
Jeffrey A Hussmann ◽  
Nicole T Schirle Oakdale ◽  
Elizabeth A Costa ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Transmembrane Domain ◽  
Transmembrane Proteins ◽  
Ribosome Profiling ◽  
Membrane Insertion ◽  
Membrane Protein Complex ◽  
Trade Off ◽  
Charged Residues ◽  
Er Membrane

The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability.

scholarly journals The ER membrane protein complex promotes biogenesis of sterol-related enzymes maintaining cholesterol homeostasis

2018 ◽  
Vol 132 (2) ◽  
pp. jcs223453 ◽  
Author(s):  
Norbert Volkmar ◽  
Maria-Laetitia Thezenas ◽  
Sharon M. Louie ◽  
Szymon Juszkiewicz ◽  
Daniel K. Nomura ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Cholesterol Homeostasis ◽  
Membrane Protein Complex ◽  
Er Membrane

scholarly journals The ER Membrane Protein Complex Promotes Biogenesis of Dengue and Zika Virus Non-structural Multi-pass Transmembrane Proteins to Support Infection

Cell Reports ◽  
2019 ◽  
Vol 27 (6) ◽  
pp. 1666-1674.e4 ◽  
Author(s):  
David L. Lin ◽  
Takamasa Inoue ◽  
Yu-Jie Chen ◽  
Aaron Chang ◽  
Billy Tsai ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Zika Virus ◽  
Protein Complex ◽  
Transmembrane Proteins ◽  
Membrane Protein Complex ◽  
Er Membrane

scholarly journals The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 624 ◽  
Author(s):  
Jeremy G. Wideman
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Common Ancestor ◽  
Eukaryotic Cells ◽  
Eukaryotic Lineage ◽  
Membrane Protein Complex ◽  
Outer Membranes ◽  
Homology Searching ◽  
Eukaryote Evolution ◽  
Er Membrane

The recently discovered endoplasmic reticulum (ER) membrane protein complex (EMC) has been implicated in ER-associated degradation (ERAD), lipid transport and tethering between the ER and mitochondrial outer membranes, and assembly of multipass ER-membrane proteins. The EMC has been studied in both animals and fungi but its presence outside the Opisthokont clade (animals + fungi + related protists) has not been demonstrated. Here, using homology-searching algorithms, I show that the EMC is truly an ancient and conserved protein complex, present in every major eukaryotic lineage. Very few organisms have completely lost the EMC, and most, even over 2 billion years of eukaryote evolution, have retained a majority of the complex members. I identify Sop4 and YDR056C in Saccharomyces cerevisiae as Emc7 and Emc10, respectively, subunits previously thought to be specific to animals. This study demonstrates that the EMC was present in the last eukaryote common ancestor (LECA) and is an extremely important component of eukaryotic cells even though its primary function remains elusive.

scholarly journals Disrupted ER membrane protein complex–mediated topogenesis drives congenital neural crest defects

2020 ◽  
Vol 130 (2) ◽  
pp. 813-826 ◽  
Author(s):  
Jonathan Marquez ◽  
June Criscione ◽  
Rebekah M. Charney ◽  
Maneeshi S. Prasad ◽  
Woong Y. Hwang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neural Crest ◽  
Protein Complex ◽  
Membrane Protein Complex ◽  
Er Membrane

scholarly journals The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 624 ◽  
Author(s):  
Jeremy G. Wideman
Keyword(s):  
Membrane Protein ◽  
Protein Complex ◽  
Common Ancestor ◽  
Eukaryotic Cells ◽  
Eukaryotic Lineage ◽  
Membrane Protein Complex ◽  
Outer Membranes ◽  
Homology Searching ◽  
Eukaryote Evolution ◽  
Er Membrane

The recently discovered endoplasmic reticulum (ER) membrane protein complex (EMC) has been implicated in ER-associated degradation (ERAD), lipid transport and tethering between the ER and mitochondrial outer membranes, and assembly of multipass ER-membrane proteins. The EMC has been studied in both animals and fungi but its presence outside the Opisthokont clade (animals + fungi + related protists) has not been demonstrated. Here, using homology-searching algorithms, I show that the EMC is truly an ancient and conserved protein complex, present in every major eukaryotic lineage. Very few organisms have completely lost the EMC, and most, even over 2 billion years of eukaryote evolution, have retained a majority of the complex members. I identify Sop4 and YDR056C in Saccharomyces cerevisiae as Emc7 and Emc10, respectively, subunits previously thought to be specific to animals. This study demonstrates that the EMC was present in the last eukaryote common ancestor (LECA) and is an extremely important component of eukaryotic cells even though its primary function remains elusive.

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