The multifaceted roles of the HORMA domain in cellular signaling
Open Access
- 23 November 2015
- journal article
- review article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 211 (4), 745-755
- https://doi.org/10.1083/jcb.201509076
Abstract
The HORMA domain is a multifunctional protein–protein interaction module found in diverse eukaryotic signaling pathways including the spindle assembly checkpoint, numerous DNA recombination/repair pathways, and the initiation of autophagy. In all of these pathways, HORMA domain proteins occupy key signaling junctures and function through the controlled assembly and disassembly of signaling complexes using a stereotypical “safety belt” peptide interaction mechanism. A recent explosion of structural and functional work has shed new light on these proteins, illustrating how strikingly similar structural mechanisms give rise to radically different functional outcomes in each family of HORMA domain proteins.Keywords
This publication has 114 references indexed in Scilit:
- Architecture of the Atg17 Complex as a Scaffold for Autophagosome BiogenesisCell, 2012
- Checkpoint mechanisms: the puppet masters of meiotic prophaseTrends in Cell Biology, 2011
- The role of the Atg1/ULK1 complex in autophagy regulationCurrent Opinion in Cell Biology, 2010
- Protein Metamorphosis: The Two-State Behavior of Mad2Structure, 2008
- MAD contortions: conformational dimerization boosts spindle checkpoint signalingCurrent Opinion in Structural Biology, 2007
- The Mad2 Conformational Dimer: Structure and Implications for the Spindle Assembly CheckpointCell, 2007
- p31comet Blocks Mad2 Activation through Structural MimicryCell, 2007
- The Mad1/Mad2 Complex as a Template for Mad2 Activation in the Spindle Assembly CheckpointCurrent Biology, 2005
- Spindle Checkpoint Protein Dynamics at Kinetochores in Living CellsCurrent Biology, 2004
- Dynamics of Centromere and Kinetochore Proteins: Implications for Checkpoint Signaling and SilencingCurrent Biology, 2004