Membrane Targeting in Secretion

  • Michael Schrader
Part of the Subcellular Biochemistry book series (SCBI, volume 37)


Regulated secretion and exocytosis require the selective packaging of regulated secretory proteins in secretory storage organelles and the controlled docking and fusion of these organelles with the plasma membrane. Secretory granule biogenesis involves sorting of secretory proteins and membrane components both at the level of the trans-Golgi network and the immature secretory granule. Sorting is thought to be mediated by selective protein aggregation and the interaction of these proteins with specific membrane domains. There is now considerable interest in the understanding of the complex lipid—protein and protein—protein interactions at the trans-Golgi network and the granule membrane. A role for lipid microdomains and associated sorting receptors in membrane targeting and granule formation is vividly discussed for (neuro)endocrine cells. In exocrine cells, however, little has been known of granule membrane composition and membrane protein function. With the cloning and characterization of granule membrane proteins and their interactions at the inner leaflet of zymogen granules of pancreatic acinar cells, it is now possible to elcuidate their function in membrane targeting and sorting of zymogens at the molecular level.


Acinar Cell Lipid Raft Secretory Granule Pancreatic Acinar Cell Exocrine Pancreas 
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.



chromogranin A, B


carboxypeptidase E


condensing vacuole








immature secretory granules




mature secretory granules


N-ethyl-maleimide-sensitive factor


prohormone convertase


phosphatidylinositolspecific phospholipase C




proline-rich proteins


regulated secretory proteins


src homology 3 domain binding motif


soluble N-ethylmaleimide-sensitive factor attachment protein


soluble N-ethyl-maleimide-sensitive factor attachment protei receptors


trans-Golgi network


Tamm-Horsfall protein


zymogen granule membrane


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Copyright information

© Springer Science+Business Media New York 2004

Authors and Affiliations

  • Michael Schrader
    • 1
  1. 1.Department of Cell Biology and Cell PathologyUniversity of MarburgMarburgGermany

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