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Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
2010 (engelsk)Inngår i: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 277, nr 22, s. 4578-4590Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The S100 proteins are 10-12 kDa EF-hand proteins that act as central regulators in a multitude of cellular processes including cell survival, proliferation, differentiation and motility. Consequently, many S100 proteins are implicated and display marked changes in their expression levels in many types of cancer, neurodegenerative disorders, inflammatory and autoimmune diseases. The structure and function of S100 proteins are modulated by metal ions via Ca(2+) binding through EF-hand motifs and binding of Zn(2+) and Cu(2+) at additional sites, usually at the homodimer interfaces. Ca(2+) binding modulates S100 conformational opening and thus promotes and affects the interaction with p53, the receptor for advanced glycation endproducts and Toll-like receptor 4, among many others. Structural plasticity also occurs at the quaternary level, where several S100 proteins self-assemble into multiple oligomeric states, many being functionally relevant. Recently, we have found that the S100A8/A9 proteins are involved in amyloidogenic processes in corpora amylacea of prostate cancer patients, and undergo metal-mediated amyloid oligomerization and fibrillation in vitro. Here we review the unique chemical and structural properties of S100 proteins that underlie the conformational changes resulting in their oligomerization upon metal ion binding and ultimately in functional control. The possibility that S100 proteins have intrinsic amyloid-forming capacity is also addressed, as well as the hypothesis that amyloid self-assemblies may, under particular physiological conditions, affect the S100 functions within the cellular milieu.

sted, utgiver, år, opplag, sider
2010. Vol. 277, nr 22, s. 4578-4590
Emneord [en]
amyloid;fibril;function;metal ions;misfolding;oligomer;self-assembly;structure;S100 proteins
Identifikatorer
URN: urn:nbn:se:umu:diva-42961DOI: 10.1111/j.1742-4658.2010.07887.xISI: 000283600300002PubMedID: 20977662OAI: oai:DiVA.org:umu-42961DiVA, id: diva2:410831
Tilgjengelig fra: 2011-04-15 Laget: 2011-04-15 Sist oppdatert: 2018-06-08bibliografisk kontrollert

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