Different functional modes of BAR domain proteins in formation and plasticity of mammalian postsynapses.
A plethora of cell biological processes involve modulations of cellular membranes. By using extended lipid-binding interfaces, some proteins have the power to shape membranes by attaching to them. Among such membrane shapers, the superfamily of Bin-Amphiphysin-Rvs (BAR) domain proteins has recently taken center stage. Extensive structural work on BAR domains has revealed a common curved fold that can serve as an extended membrane-binding interface to modulate membrane topologies and has allowed the grouping of the BAR domain superfamily into subfamilies with structurally slightly distinct BAR domain subtypes (N-BAR, BAR, F-BAR and I-BAR). Most BAR superfamily members are expressed in the mammalian nervous system. Neurons are elaborately shaped and highly compartmentalized cells. Therefore, analyses of synapse formation and of postsynaptic reorganization processes (synaptic plasticity) - a basis for learning and memory formation - has unveiled important physiological functions of BAR domain superfamily members. These recent advances, furthermore, have revealed that the functions of BAR domain proteins include different aspects. These functions are influenced by the often complex domain organization of BAR domain proteins. In this Commentary, we review these recent insights and propose to classify BAR domain protein functions into (1) membrane shaping, (2) physical integration, (3) action through signaling components, and (4) suppression of other BAR domain functions.
Institute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University, Nonnenplan 2-4, 07743 Jena, Germany Britta.Qualmann@med.uni-jena.de Michael.Kessels@med.uni-jena.de.
Michael M
MM
Kessels
Institute of Biochemistry I, Jena University Hospital/Friedrich-Schiller-University, Nonnenplan 2-4, 07743 Jena, Germany Britta.Qualmann@med.uni-jena.de Michael.Kessels@med.uni-jena.de.
Britta
B
Qualmann
D000818:Animals; D049229:Dendritic Spines / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D013569:Synapses / Q000235:genetics / Q000378:metabolism*
D008565:Membrane Proteins; D009419:Nerve Tissue Proteins
BAR domain proteins; Dendritic spine shape; Glutamate receptor; Postsynaptic plasticity; Synapse formation