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Sci. Signal., 21 July 2009
Vol. 2, Issue 80, p. ec248
[DOI: 10.1126/scisignal.280ec248]

EDITORS' CHOICE

Cell Biology Plethora of Secretory Amyloids

Stella M. Hurtley

Science, AAAS, Cambridge CB2 1LQ, UK

Protein aggregation and the formation of amyloids are associated with several dozen pathological conditions in humans, including Alzheimer’s disease, Parkinson’s disease, and type II diabetes. In addition, a few functional amyloid systems are known: the prions of fungi, the bacterial protein curli, the protein chorion of the eggshell of silkworm, and the amyloid protein Pmel-17 involved in mammalian skin pigmentation. Now Maji et al. propose that endocrine hormone peptides and proteins are stored in an amyloid-like state in secretory granules. Thus, the amyloid fold may represent a fundamental, ancient, and evolutionarily conserved protein structural motif that is capable of performing a wide variety of functions contributing to normal cell and tissue physiology.

S. K. Maji, M. H. Perrin, M. R. Sawaya, S. Jessberger, K. Vadodaria, R. A. Rissman, P. S. Singru, K. P. R. Nilsson, R. Simon, D. Schubert, D. Eisenberg, J. Rivier, P. Sawchenko, W. Vale, R. Riek, Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328–332 (2009). [Abstract] [Full Text]

Citation: S. M. Hurtley, Plethora of Secretory Amyloids. Sci. Signal. 2, ec248 (2009).


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