Domains of the TGN: Coats, tethers and G proteins


Autoria(s): Gleeson, Paul A.; Lock, John G.; Luke, Michael R.; Stow, Jennifer L.
Data(s)

01/05/2004

Resumo

The trans-Golgi network is the major sorting compartment of the secretory pathway for protein, lipid and membrane traffic. There is a constant flow of membrane and cargo to and from this compartment. Evidence is emerging that the trans-Golgi network has multiple biochemically and functionally distinct subdomains, each of which contributes to the combined sorting and transport requirements of this dynamic compartment. The recruitment of distinct arrays of protein complexes to trans-Golgi network membranes is likely to produce the diversity of structure and biochemistry observed amongst subdomains that serve to generate different carriers or maintain resident trans-Golgi network components. This review discusses how these subdomains may be formed and examines the molecular players involved, including G proteins, clathrin adaptors and golgin tethers. Diversity within these protein families is highlighted and shown to be critical for the functionality of the trans-Golgi network, as a mediator of protein sorting and membrane transport, and for the maintenance of Golgi structure.

Identificador

http://espace.library.uq.edu.au/view/UQ:73517

Idioma(s)

eng

Publicador

John Wiley & Sons

Palavras-Chave #Cell Biology #Adaptors #Adp-ribosylation Factor #Arl #Clathrin #Coats #Golgins #Grip Domain #Membrane Subdomains #Membrane Transport #Trans-golgi Network #Mannose 6-phosphate Receptors #Coiled-coil Proteins #Llc-pk1 Epithelial-cells #Ap-3 Adapter Complex #Distinct Membrane Domains #Clathrin Binding Subunit #Darby Canine Kidney #Ear Homology Domain #C1 #270103 Protein Targeting and Signal Transduction #780106 Political science and public policy
Tipo

Journal Article