Antibodies Secretion

Roberto Sitia, DIBIT - San Raffaele Scientific Institute, 20132 Milan, Italy

Copyright © 1998 Elsevier Ltd. All Rights Reserved.

As established by the classical experiments of Palade and coworkers, proteins destined to be secreted (as well as cell surface proteins) are synthesized in the endoplasmic reticulum (ER), and then transported through the Golgi complex to the extracellular space. Distinct post-translational modifications (assembly, glycosylation, etc.) take place sequentially along this pathway, allowing the intracellular location of a protein to be determined. The stepwise nature of the secretory pathway is confirmed by the existence of drugs which block intracellular transport at given stages. Similarly, several yeast temperature-sensitive mutants have been characterized in which secretion is blocked at different levels. Since mutations or drugs block the export of most secretory proteins, there appears to be only one main secretory pathway, utilized also by proteins destined to be expressed on the plasma membrane. An alternative pathway has been identified, which allows the selective secretion of certain cytosolic proteins lacking a conventional 'signal sequence' (see below).

Antibody secretion will be discussed in the context of the general problems of protein secretion. Among the many exciting questions in this field, the ones related to selectivity are maybe the most intriguing. How do cells decide what to secrete, when, and for how long?

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