Zobrazeno 1 - 10
of 102
pro vyhledávání: '"Hans-Peter Hauri"'
Publikováno v:
Molecular Biology of the Cell
In search of morphological determinants for the endoplasmic reticulum-Golgi intermediate compartment (ERGIC), we found that a concerted action of Arf1, Arf4, and PLA2G6-A controls the architecture of the ERGIC by regulating tubular carriers. This is
Publikováno v:
Journal of Cell Science. 123:1705-1715
Selective export of transmembrane proteins from the endoplasmic reticulum (ER) relies on recognition of cytosolic-domain-localized transport signals by the Sec24 subunit of the COPII vesicle coat. Human cells express four Sec24 isoforms, termed Sec24
Publikováno v:
Traffic. 11:1044-1055
The leguminous-type (L-type) lectin VIP36 localizes to the Golgi apparatus and cycles early in the secretory pathway. In vitro, VIP36 binds high-mannose glycans with a pH optimum of 6.5, a value similar to the luminal pH of the Golgi apparatus. Altho
Autor:
Carine Bonnon, Sandra Mitrovic, Regula Halbeisen, Hans-Peter Hauri, Eva Koegler, Lorenz Waldmeier
Publikováno v:
Traffic. 11:70-89
The mammalian Golgi apparatus consists of individual cisternae that are stacked in a polarized manner to form the compact zones of the Golgi. Several stacks are linked to form a ribbon via dynamic lateral bridges. The determinants required for mainta
Autor:
Mitsuo Tagaya, Akitsugu Yamamoto, Katsuko Tani, Nagisa Arimitsu, Takehiro Aoki, Takayuki Iinuma, Kohei Arasaki, Rie Samata, Hidenori Hirose, Hans-Peter Hauri
Publikováno v:
Journal of Cell Science. 122:1680-1690
The presence of subdomains in the endoplasmic reticulum (ER) enables this organelle to perform a variety of functions, yet the mechanisms underlying their organization are poorly understood. In the present study, we show that syntaxin 18, a SNAP (sol
Autor:
Michael Freissmuth, Susanne Maier, Hesso Farhan, Harald H. Sitte, Alexander Kriz, Hans-Peter Hauri, Veronika Reiterer, Markus A. Rüegg
Publikováno v:
The Journal of Neuroscience. 28:12453-12464
The GABA transporter-1 (GAT1) is a prototypical protein of the synaptic specialization. Export of GAT1 from the endoplasmic reticulum (ER) is contingent on its interaction with the COPII (coatomer protein-II) coat subunit Sec24D. Here we show that si
Publikováno v:
The EMBO Journal. 27:2043-2054
The biogenesis of endoplasmic reticulum (ER) exit sites (ERES) involves the formation of phosphatidylinositol-4 phosphate (PI4) and Sec16, but it is entirely unknown how ERES adapt to variations in cargo load. Here, we studied acute and chronic adapt
Autor:
Sawako Takai, Mitsuo Tagaya, Hans-Peter Hauri, David J. Stephens, Ken-ichi Nakajima, Peter Duncan Watson, Katsuko Tani, Yuichi Wakana, Akitsugu Yamamoto
Publikováno v:
Molecular Biology of the Cell. 19:1825-1836
Certain endoplasmic reticulum (ER)-associated degradation (ERAD) substrates with transmembrane domains are segregated from other ER proteins and sorted into a juxtanuclear subcompartment, known as the ER quality control compartment. Bap31 is an ER pr
Autor:
Hans-Peter Hauri, Harald H. Sitte, Margit Pavelka, Hesso Farhan, Veronika Reiterer, Michael Freissmuth, Alexander Kriz
Publikováno v:
Journal of Cell Science. 121:753-761
The C-terminus of GABA transporter 1 (GAT1, SLC6A1) is required for trafficking of the protein through the secretory pathway to reach its final destination, i.e. the rim of the synaptic specialization. We identified a motif of three hydrophobic resid
Autor:
Markus W. Wendeler, Veronika Reiterer, Hans Peter Hauri, Beat Nyfeler, Stephen W. Michnick, Bin Zhang, Eduard Stefan
Publikováno v:
The Journal of Cell Biology
Secretory proteins are exported from the endoplasmic reticulum (ER) by bulk flow and/or receptor-mediated transport. Our understanding of this process is limited because of the low number of identified transport receptors and cognate cargo proteins.