PUBLICATION
Structural Insights into the Organization of the Cavin Membrane Coat Complex
- Authors
- Kovtun, O., Tillu, V.A., Jung, W., Leneva, N., Ariotti, N., Chaudhary, N., Mandyam, R.A., Ferguson, C., Morgan, G.P., Johnston, W.A., Harrop, S.J., Alexandrov, K., Parton, R.G., Collins, B.M.
- ID
- ZDB-PUB-141203-39
- Date
- 2014
- Source
- Developmental Cell 31: 405-419 (Journal)
- Registered Authors
- Parton, Robert G.
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Caveolae/chemistry*
- Caveolae/metabolism*
- Caveolae/ultrastructure
- Caveolins/chemistry*
- Caveolins/metabolism*
- Crystallography, X-Ray
- Cytoplasm/chemistry
- Cytoplasm/metabolism*
- Cytoplasm/ultrastructure
- Membrane Proteins/metabolism
- Microscopy, Electron
- Molecular Sequence Data
- Protein Structure, Quaternary
- RNA-Binding Proteins/chemistry*
- RNA-Binding Proteins/metabolism*
- Signal Transduction/physiology
- Zebrafish/metabolism
- PubMed
- 25453557 Full text @ Dev. Cell
Citation
Kovtun, O., Tillu, V.A., Jung, W., Leneva, N., Ariotti, N., Chaudhary, N., Mandyam, R.A., Ferguson, C., Morgan, G.P., Johnston, W.A., Harrop, S.J., Alexandrov, K., Parton, R.G., Collins, B.M. (2014) Structural Insights into the Organization of the Cavin Membrane Coat Complex. Developmental Cell. 31:405-419.
Abstract
Caveolae are cell-surface membrane invaginations that play critical roles in cellular processes including signaling and membrane homeostasis. The cavin proteins, in cooperation with caveolins, are essential for caveola formation. Here we show that a minimal N-terminal domain of the cavins, termed HR1, is required and sufficient for their homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved trimeric coiled-coil architectures, with intersubunit interactions that determine the specificity of cavin-cavin interactions. The HR1 domain contains a basic surface patch that interacts with polyphosphoinositides and coordinates with additional membrane-binding sites within the cavin C terminus to facilitate membrane association and remodeling. Electron microscopy of purified cavins reveals the existence of large assemblies, composed of a repeating rod-like structural element, and we propose that these structures polymerize through membrane-coupled interactions to form the unique striations observed on the surface of caveolae in vivo.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
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Orthology
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