Abstract
Proteins destined to be secreted via the regulated pathway are synthesized in the endoplasmic reticulum (ER), transit through the various cisternae of the Golgi apparatus where they become modified, and finally are stored in secretory granules. Under stimulation of the cells, secretory granules fuse with the apical plasma membrane, and their content is released into the extracellular medium. It is now well established that every step of the transport occurring between these different compartments involves vesicular carriers,1 but the role of the cytoskeleton in the secretory pathway is still under discussion. In many cell types, the rate of the intracellular traffic of proteins is reduced in the presence of microtubule depolymerizing agents, so microtubules were first thought to play a role in the movement of the secretory vesicles.2 Recent in vitro results have shown that vesicle budding, movement, and fusion do not require the cytoskeleton, so the microtubules are now considered mainly to play a role in the maintenance of a correct location of the organelles rather than in a direct guiding of the secretory vesicles.3
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References
Rothman JE, Wieland FT. Protein sorting by transport vesicles. Science. 1996; 272: 227–234.
Burgess TL, Kelly RB. Constitutive and regulated secretion of proteins. Annu Rev Cell Biol. 1987; 3: 243–293.
Allan V. Membrane traffic motors. FEBS Lett. 1995; 369: 101–106.
Busson-Mabillot S, Chambault-Guerin AM, Ovtracht L, Muller P, Rossignol B. Microtubules and protein secretion in rat lacrimal glands: localization of short term effects of colchicine on the secretory process. J Cell Biol. 1982; 95: 105–117.
Donaldson JG, Lippincott-Schwartz J, Bloom GS, Kreis TE, Klausner RD. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J Cell Biol. 1990; 111: 2295–2306.
Cole NB, Lippincott-Schwartz J. Organization of organelles and membrane traffic by microtubules. Curr Opin Cell Biol. 1995; 7: 55–64.
Robin P, Rossignol B, Raymond M-N. Recovery of protein secretion after brefeldin A treatment of rat lacrimal glands: Effect of cAMP. Am J Physiol. 1996; 271: C783 - C793.
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Robin, P., Raymond, MN., Rossignol, B. (1998). Microtubules and Intracellular Traffic of Secretory Proteins in Rat Extraorbital Lacrimal Glands. In: Sullivan, D.A., Dartt, D.A., Meneray, M.A. (eds) Lacrimal Gland, Tear Film, and Dry Eye Syndromes 2. Advances in Experimental Medicine and Biology, vol 438. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5359-5_19
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DOI: https://doi.org/10.1007/978-1-4615-5359-5_19
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