Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization

Hafumi Nishi, Kosuke Hashimoto, Thomas Madej, Anna R. Panchenko

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

30 Citations (Scopus)

Abstract

Protein homooligomers afford several important benefits for the cell; they mediate and regulate gene expression, activity of many enzymes, ion channels, receptors, and cell-cell adhesion processes. The evolutionary and physical mechanisms of oligomer formation are very diverse and are not well understood. Certain homooligomeric states may be conserved within protein subfamilies and between different subfamilies, therefore providing the specificity to particular substrates while minimizing interactions with unwanted partners. In addition, transitions between different oligomeric states may regulate protein activity and support the switch between different pathways. In this chapter, we summarize the biological importance of homooligomeric assemblies, physicochemical properties of their interfaces, experimental methods for their identification, their evolution, and role in human diseases.

Original languageEnglish
Title of host publicationOligomerization in Health and Disease
PublisherElsevier B.V.
Pages3-24
Number of pages22
ISBN (Print)9780123869319
DOIs
Publication statusPublished - 2013

Publication series

NameProgress in Molecular Biology and Translational Science
Volume117
ISSN (Print)1877-1173

Keywords

  • Cellular regulation
  • Disease
  • Evolution
  • Protein aggregation
  • Protein interaction
  • Protein oligomer

Fingerprint

Dive into the research topics of 'Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization'. Together they form a unique fingerprint.

Cite this