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- Publications
- Influence
The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
- Christian Appenzeller-Herzog, H. Hauri
- Biology, Medicine
- Journal of Cell Science
- 1 June 2006
Protein traffic moving from the endoplasmic reticulum (ER) to the Golgi complex in mammalian cells passes through the tubulovesicular membrane clusters of the ER-Golgi intermediate compartment… Expand
Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
- Markus W. Wendeler, J. Paccaud, H. Hauri
- Biology, Medicine
- EMBO reports
- 1 March 2007
Sec24 of the COPII (coat protein complex II) vesicle coat mediates the selective export of membrane proteins from the endoplasmic reticulum (ER) in yeast. Human cells express four Sec24 isoforms, but… Expand
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
- C. Appenzeller, H. Andersson, F. Kappeler, H. Hauri
- Chemistry, Medicine
- Nature Cell Biology
- 1 October 1999
Soluble secretory proteins are transported from the endoplasmic reticulum (ER) to the ER–Golgi intermediate compartment (ERGIC) in vesicles coated with COP-II coat proteins. The sorting of secretory… Expand
Selective export of human GPI-anchored proteins from the endoplasmic reticulum
- Carine Bonnon, Markus W. Wendeler, J. Paccaud, H. Hauri
- Biology, Medicine
- Journal of Cell Science
- 15 May 2010
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.… Expand
Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules.
- C. Vedrenne, D. Klopfenstein, H. Hauri
- Biology, Medicine
- Molecular biology of the cell
- 9 February 2005
The microtubule-binding 63-kDa cytoskeleton-linking membrane protein (CLIMP-63) is an integral membrane protein that links the endoplasmic reticulum (ER) to microtubules. Here, we tested whether this… Expand
Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
- H. Farhan, Matthias Weiss, K. Tani, R. Kaufman, H. Hauri
- Biology, Medicine
- The EMBO journal
- 6 August 2008
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… Expand
The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles
- M. Muñiz, C. Nuoffer, H. Hauri, H. Riezman
- Biology, Medicine
- The Journal of cell biology
- 6 March 2000
Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex required for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi… Expand
MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening
- H. Farhan, Markus W. Wendeler, +5 authors H. Hauri
- Biology, Medicine
- The Journal of cell biology
- 14 June 2010
An RNAi screen determines that the early secretory pathway is subject to phosphoregulation via a variety of signaling pathways, including a link between growth factor signaling and ER export.
Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export.
- O. Nufer, Svend Guldbrandsen, +4 authors H. Hauri
- Biology, Medicine
- Journal of cell science
- 1 February 2002
Export of membrane proteins from the ER is believed to be selective and require transport signals, but the identity of such signals has remained elusive. The recycling type I membrane protein… Expand
Capturing protein interactions in the secretory pathway of living cells.
- B. Nyfeler, S. Michnick, H. Hauri
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 3 May 2005
The secretory pathway is composed of membrane compartments specialized in protein folding, modification, transport, and sorting. Numerous transient protein-protein interactions guide the… Expand