Creativity comes from interactions: modules of protein interactions in plants.

Journal Article (Review;Journal Article)

Protein interactions are the foundation of cell biology. For robust signal transduction to occur, proteins interact selectively and modulate their behavior to direct specific biological outcomes. Frequently, modular protein interaction domains are central to these processes. Some of these domains bind proteins bearing post-translational modifications, such as phosphorylation, whereas other domains recognize and bind to specific amino acid motifs. Other modules act as diverse protein interaction scaffolds or can be multifunctional, forming head-to-head homodimers and binding specific peptide sequences or membrane phospholipids. Additionally, the so-called head-to-tail oligomerization domains (SAM, DIX, and PB1) can form extended polymers to regulate diverse aspects of biology. Although the mechanism and structures of these domains are diverse, they are united by their modularity. Together, these domains are versatile and facilitate the evolution of complex protein interaction networks. In this review, we will highlight the role of select modular protein interaction domains in various aspects of plant biology.

Full Text

Duke Authors

Cited Authors

  • Allen, JR; Wilkinson, EG; Strader, LC

Published Date

  • March 2022

Published In

Volume / Issue

  • 289 / 6

Start / End Page

  • 1492 - 1514

PubMed ID

  • 33774929

Pubmed Central ID

  • PMC8476656

Electronic International Standard Serial Number (EISSN)

  • 1742-4658

International Standard Serial Number (ISSN)

  • 1742-464X

Digital Object Identifier (DOI)

  • 10.1111/febs.15847


  • eng