Cargando…

N-acetylation and phosphorylation of Sec complex subunits in the ER membrane

BACKGROUND: Covalent modifications of proteins provide a mechanism to control protein function. Here, we have investigated modifications of the heptameric Sec complex which is responsible for post-translational protein import into the endoplasmic reticulum (ER). It consists of the Sec61 complex (Sec...

Descripción completa

Detalles Bibliográficos
Autores principales:	Soromani, Christina, Zeng, Naiyan, Hollemeyer, Klaus, Heinzle, Elmar, Klein, Marie-Christine, Tretter, Thomas, Seaman, Matthew N J, Römisch, Karin
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	BioMed Central 2012
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3541991/ https://www.ncbi.nlm.nih.gov/pubmed/23237413 http://dx.doi.org/10.1186/1471-2121-13-34

Ejemplares similares

The N-terminus of Sec61p plays key roles in ER protein import and ERAD
por: Elia, Francesco, et al.
Publicado: (2019)

Sec61 channel subunit Sbh1/Sec61β promotes ER translocation of proteins with suboptimal targeting sequences and is fine-tuned by phosphorylation
por: Barbieri, Guido, et al.
Publicado: (2023)

Analysis of Sec61p and Ssh1p interactions in the ER membrane using the split-ubiquitin system
por: Harty, Carol, et al.
Publicado: (2013)

ERAD and protein import defects in a sec61 mutant lacking ER-lumenal loop 7
por: Tretter, Thomas, et al.
Publicado: (2013)

How does Sec63 affect the conformation of Sec61 in yeast?
por: Bhadra, Pratiti, et al.
Publicado: (2021)

The Sec63p J-Domain Is Required for ERAD of Soluble Proteins in Yeast
por: Servas, Christina, et al.
Publicado: (2013)

CK2 Phosphorylates Sec31 and Regulates ER-To-Golgi Trafficking
por: Koreishi, Mayuko, et al.
Publicado: (2013)

Proteasome 19S RP Binding to the Sec61 Channel Plays a Key Role in ERAD
por: Kaiser, Marie-Luise, et al.
Publicado: (2015)

Sec16 function in ER export and autophagy is independent of its phosphorylation in Saccharomyces cerevisiae
por: Yorimitsu, Tomohiro, et al.
Publicado: (2020)

Sec12 Binds to Sec16 at Transitional ER Sites
por: Montegna, Elisabeth A., et al.
Publicado: (2012)

MoSec61β, the beta subunit of Sec61, is involved in fungal development and pathogenicity, plant immunity, and ER-phagy in Magnaporthe oryzae
por: Wei, Yun-Yun, et al.
Publicado: (2020)

The ER Protein Translocation Channel Subunit Sbh1 Controls Virulence of Cryptococcus neoformans
por: Santiago-Tirado, Felipe H., et al.
Publicado: (2023)

Diversion at the ER: How Plasmodium falciparum exports proteins into host erythrocytes
por: Römisch, Karin
Publicado: (2012)

Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation
por: Pereira, Fabio, et al.
Publicado: (2019)

Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
por: Morgera, Francesca, et al.
Publicado: (2012)

Large-Scale Evolutionary Analyses on SecB Subunits of Bacterial Sec System
por: Yan, Shaomin, et al.
Publicado: (2015)

ULK1 phosphorylates Sec23A and mediates autophagy-induced inhibition of ER-to-Golgi traffic
por: Gan, Wenjia, et al.
Publicado: (2017)

Sec61β, a subunit of the Sec61 protein translocation channel at the Endoplasmic Reticulum, is involved in the transport of Gurken to the plasma membrane.
por: Kelkar, Anshuman, et al.
Publicado: (2009)

Evolutionary Gain of Function for the ER Membrane Protein Sec62 from Yeast to Humans
por: Müller, Linda, et al.
Publicado: (2010)

Sec18 supports membrane fusion by promoting Sec17 membrane association
por: Orr, Amy, et al.
Publicado: (2022)

SEC23A confers ER stress resistance in gastric cancer by forming the ER stress-SEC23A-autophagy negative feedback loop
por: Cheng, Quan, et al.
Publicado: (2023)

Sec35p, a Novel Peripheral Membrane Protein, Is Required for ER to Golgi Vesicle Docking
por: VanRheenen, Susan M., et al.
Publicado: (1998)

SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane
por: Jüschke, Christoph, et al.
Publicado: (2005)

Cell cycle–dependent phosphorylation of Sec4p controls membrane deposition during cytokinesis
por: Lepore, Dante, et al.
Publicado: (2016)

Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit
por: Zhao, Xueqiang, et al.
Publicado: (2009)

Crystal structure of Sec10, a subunit of the exocyst complex
por: Chen, Jianxing, et al.
Publicado: (2017)

Two subunits of the exocyst, Sec3p and Exo70p, can function exclusively on the plasma membrane
por: Liu, Dongmei, et al.
Publicado: (2018)

p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport
por: Ong, Yan Shan, et al.
Publicado: (2010)

Stage- and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane
Publicado: (1995)

Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane
por: Dajkovic, Alex, et al.
Publicado: (2016)

Acetylated microtubules let the ER slide
por: Short, Ben
Publicado: (2010)

Cancer associated mutations in Sec61γ alter the permeability of the ER translocase
por: Witham, Christopher M., et al.
Publicado: (2021)

Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation
por: Davis, Saralin, et al.
Publicado: (2016)

ER sliding dynamics and ER–mitochondrial contacts occur on acetylated microtubules
por: Friedman, Jonathan R., et al.
Publicado: (2010)

Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
por: Kaiser, Christina, et al.
Publicado: (2004)

Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes
por: Song, Hongki, et al.
Publicado: (2017)

The endoplasmic reticulum membrane protein Sec62 as potential therapeutic target in SEC62 overexpressing tumors
por: Zimmermann, Julia S. M., et al.
Publicado: (2022)

O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport
por: Seepersaud, Ravin, et al.
Publicado: (2017)

Cryo–EM structure of the ribosome–SecYE complex in the membrane environment
por: Frauenfeld, Jens, et al.
Publicado: (2011)

Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins
por: Scott, Daniel C., et al.
Publicado: (2008)

Cannot write session to /tmp/vufind_sessions/sess_cva9raeq4pcgaik3mn2ji7rnn4