Protein sorting and vesicular traffic in the Golgi apparatus

  • M. G. Farquhar
  • H.-P. Hauri
Part of the Molecular and Cell Biology Updates book series (MCBU)


During the last ten to 15 years there has been an explosion of new information on mechanisms of protein sorting and vesicular traffic along the exocytic pathway, that has allowed us to extend and modify earlier models. We now know that newly synthesized proteins translocated to the endoplasmatic reticulum (ER) are not automatically transported to the Golgi stack. They must pass through an elaborate ER quality control system which assures that they are properly folded and assembled before leaving the ER. We also have learned that resident ER proteins are normally retained in the ER by mechanisms that are still poorly understood, but if they happen to escape they are retrieved by binding to receptors located in thecis-Golgi and transported back to the ER. A new compartment, the ER to Golgi intermediate compartment (ERGIC), with distinct morphological and biochemical features, has been discovered. In mammalian cells cargo is shuttled from the ER to ERGIC via one type of vesicle (COP II-coated vesicles) and from ERGIC to thecis-Golgi network via another (presumably COP I-coated vesicles). It has long been postulated that cargo exits the ER at specific sites, the transitional ER elements, and that transport is nonselective and occurs by so-called “bulk-flow”. However, there is growing evidence that proteins are sorted for packaging into carrier vesicles rather than being transported by bulk-flow. Cargo undergoes concentration (five to ten times) at the time of exit. The mechanism by which cargo is transported through the GA fromcis totrans remains to be elucidated. According to one model it is mediated by vesicular transport. Another view is that transport my occur by cisternal progression whereby thecis-cisterna gradually matures to become the transmost cisterna. Cargo is modified in transit by Golgi-specific post-translational modifications (glycosylation, phosphorylation, sulfation, etc.), but no further concentration takes place until proteins reach thetrans cisternae and TGN. There, newly synthesized proteins are selectively packaged into at least four different containers — i.e. secretory granules, two types of constitutive secretory vesicles (apical and basolateral cognate), and clathrin-coated vesicles carrying lysosomal enzymes. The mechanisms of sorting are best understood in the case of lysosomal enzymes sorted via mannose 6-phosphate receptors. Sorting into regulated granules is believed to occur by aggregation, and sorting of at least some proteins into constitutive vesicles by tyrosine-based signals. The mechanisms by which resident Golgi proteins are retained in the Golgi stacks are still poorly understood, but there is a general consensus that important information resides in the transmembrane domain of integral membrane proteins. During the last few years information derived from the study of Golgi transportin vitro, yeastsec mutants, and synaptic vesicles has converged and demonstrated that vesicles involved in transport at different steps along the exocytic pathway have common features. Most have prominent coats of which there are several types. It is thought that vesicle budding is initiated by the assembly of the protein coat, thus triggering assembly of elaborate membrane and cytosolic protein complexes, unique for each vesicle population, that drive vesicle budding and fission. Included in the forming vesicle are cargo proteins, cargo receptors and membrane proteins required for vesicle docking. Pairs of integral vesicle and target membrane proteins (v-SNARES and t-SNARES), with specific family members assigned to different stations, assure docking to the appropriate membrane receptor. Soluble cytosolic proteins (NSF and SNAPs) serve as common fusion machinery for different vesicle relays. An exception is represented by the vesicles involved in apical delivery of proteins in polarized secretory cells where glycolipids and glycans appear to be involved. Attention is currently focused on how traffic is regulated and how signals are transduced from one cell compartment to the other. Small GTPases of the Rab and ARF families, heterotrimeric G proteins, and phosphoinositides are known to be involved, but understanding of their specific roles is still fragmentary.


Golgi Apparatus Protein Sorting Golgi Membrane Golgi Cisterna Vesicle Docking 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Basel AG 1997

Authors and Affiliations

  • M. G. Farquhar
    • 1
  • H.-P. Hauri
    • 2
  1. 1.Division of Cellular and Molecular Medicine and Department of PathologyUniversity of CaliforniaSan DiegoUSA
  2. 2.Department of Pharmacology, BiozentrumUniversity of BaselBaselSwitzerland

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