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Sci. Signal., 21 July 2009
Vol. 2, Issue 80, p. pe43
Functional Amyloids Signal Their Arrival
Matthew P. Badtke,
Neal D. Hammer, and
Matthew R. Chapman*
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Amyloids have traditionally been associated with misfolded protein aggregates and debilitating neurodegenerative diseases. However, a growing number of functional amyloids have now been described that demonstrate that amyloid formation can be an integral part of normal cellular physiology. Functional amyloid production is highly regulated, and the resulting fibers serve a variety of roles for the cells that produce them. A new role for amyloid as storage reservoirs for peptide hormones within mammalian secretory granules has been discovered. More than 30 different peptide hormones have been found to form amyloids in vitro, and both rats and mice have been shown to store hormone amyloid deposits in secretory granules. Thus, the emerging evidence adds to the diverse roles of amyloid and raises intriguing questions for both the peptide hormone and the functional amyloid fields.
Samir K. Maji, Marilyn H. Perrin, Michael R. Sawaya, Sebastian Jessberger, Krishna Vadodaria, Robert A. Rissman, Praful S. Singru, K. Peter R. Nilsson, Rozalyn Simon, David Schubert, David Eisenberg, Jean Rivier, Paul Sawchenko, Wylie Vale, and Roland Riek (17 July 2009) Science325 (5938), 328.
[DOI: 10.1126/science.1173155] |Abstract »|Full Text »|PDF »|Supporting Online Material »
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Promiscuous Cross-seeding between Bacterial Amyloids Promotes Interspecies Biofilms.
Y. Zhou, D. Smith, B. J. Leong, K. Brannstrom, F. Almqvist, and M. R. Chapman (2012)
J. Biol. Chem.
|Abstract »|Full Text »|PDF »
Microcin Amyloid Fibrils A Are Reservoir of Toxic Oligomeric Species.