Article
The GOLD domain, a novel protein module involved in Golgi function and secretion.
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
Genome biology (impact factor:
6.63).
02/2002;
3(5):research0023.
pp.research0023
Source: PubMed
-
Article: Protein transport from the endoplasmic reticulum to the Golgi apparatus.
[show abstract] [hide abstract]
ABSTRACT: As the first step of protein transport along the biosynthetic (secretory/exocytotic) pathway, transport from the endoplasmic reticulum (ER) to the Golgi apparatus has received much attention over the past several decades. The general structural organization underlying this transport process is becoming more defined. The major protein components participating in the budding, pre-docking, and docking/fusion events have been identified and their mechanistic aspects investigated. Conceptually, it is now clear that protein export from the ER is a selective process. Although much remains to be defined or refined, the general picture of this transport step has now emerged.Journal of Cell Science 11/1998; 111 ( Pt 19):2831-9. · 6.11 Impact Factor -
Article: Getting into the Golgi.
[show abstract] [hide abstract]
ABSTRACT: The intermediate compartment residing between the endoplasmic reticulum (ER) and the Golgi is now recognized to be a dynamic structure that captures cargo released from the ER in COPII vesicular carriers and promotes recycling by COPI vesicular carriers. These and other findings now provide compelling evidence for the importance of this intermediate in balancing anterograde and retrograde flow through the early secretory pathway and in the formation and maintenance of the Golgi stack.Trends in Cell Biology 02/1998; 8(1):21-5. · 12.35 Impact Factor -
Article: The organization of endoplasmic reticulum export complexes.
[show abstract] [hide abstract]
ABSTRACT: Export of cargo from the ER occurs through the formation of 60-70nm COPII-coated vesicular carriers. We have applied serial-thin sectioning and stereology to quantitatively characterize the three-dimensional organization of ER export sites in vivo and in vitro. We find that ER buds in vivo are nonrandomly distributed, being concentrated in regional foci we refer to as export complexes. The basic organization of an export complex can be divided into an active COPII-containing budding zone on a single ER cisterna, which is adjacent to budding zones found on distantly connected ER cisternae. These budding foci surround and face a central cluster of morphologically independent vesicular-tubular elements that contain COPI coats involved in retrograde transport. Vesicles within these export complexes contain concentrated cargo molecules. The structure of vesicular-tubular clusters in export complexes is particularly striking in replicas generated using a quick-freeze, deep-etch approach to visualize for the first time their three-dimensional organization and cargo composition. We conclude that budding from the ER through recruitment of COPII is confined to highly specialized export complexes that topologically restrict anterograde transport to regional foci to facilitate efficient coupling to retrograde recycling by COPI.The Journal of Cell Biology 11/1996; 135(1):19-35. · 10.26 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed.
The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual
current impact factor.
Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence
agreement may be applicable.
Keywords
bind membranes
cargo molecules
detected group
diverse protein-protein interactions
endoplasmic reticulum
FYVE domains
GOLD domain
GOLD-domain proteins
Golgi complex
Golgi dynamics
membrane-associated complexes
membrane-association domains
novel beta-strand-rich domain
novel class
p24 proteins
p24 proteins form hetero-oligomeric complexes
pleckstrin homology
secretion process
sensitive sequence-profile analysis methods
specific secretory cargo