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Membrane Targeting in Secretion

  • Chapter
Membrane Dynamics and Domains

Part of the book series: Subcellular Biochemistry ((SCBI,volume 37))

Abstract

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.

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Abbreviations

CgA,B:

chromogranin A, B

CPE:

carboxypeptidase E

CV:

condensing vacuole

GAG:

glucosaminoglycan

GP:

glycoprotein

GPI:

glycosylphosphatidylinositol

ISGs:

immature secretory granules

MĂźCD:

methyl-β-cyclodextrin

MSGs:

mature secretory granules

NSF:

N-ethyl-maleimide-sensitive factor

PC:

prohormone convertase

PI-PLC:

phosphatidylinositolspecific phospholipase C

POMC:

pro-opiomelanocortin

PRPs:

proline-rich proteins

RSPs:

regulated secretory proteins

SH3:

src homology 3 domain binding motif

SNAP:

soluble N-ethylmaleimide-sensitive factor attachment protein

SNAREs:

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

TGN:

trans-Golgi network

THP:

Tamm-Horsfall protein

ZGM:

zymogen granule membrane

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  1. Department of Cell Biology and Cell Pathology, University of Marburg, Robert Koch Str. 6, 35037, Marburg, Germany

    Michael Schrader

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    Peter J. Quinn

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Schrader, M. (2004). Membrane Targeting in Secretion. In: Quinn, P.J. (eds) Membrane Dynamics and Domains. Subcellular Biochemistry, vol 37. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5806-1_12

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