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In biology, caveolae (Latin for "little caves"; singular, caveola), which are a special type of lipid raft, are small (50–100 nanometer) invaginations of the plasma membrane in many vertebrate cell types, especially in endothelial cells and adipocytes.
These flask-shaped structures are rich in proteins as well as lipids such as cholesterol and sphingolipids and have several functions in signal transduction.[1] They are also believed to play a role in endocytosis, oncogenesis, and the uptake of pathogenic bacteria and certain viruses.[2][3][4]
Contents
- 1 Caveolins
- 2 Caveolar endocytosis
- 3 Other roles of caveolae
- 4 Inhibitors
- 5 See also
- 6 References
- 7 External links
Caveolins
Formation and maintenance of caveolae is primarily due to the protein caveolin,[5] a 21 kD protein. There are three homologous genes of caveolin expressed in mammalian cells: Cav1, Cav2 and Cav3. These proteins have a common topology: cytoplasmic N-terminus with scaffolding domain, long hairpin transmembrane domain and cytoplasmic C-terminus. Caveolins are synthesized as monomers and transported to the Golgi apparatus. During their subsequent transport through the secretory pathway, caveolins associate with lipid rafts and form oligomers (14-16 molecules). These oligomerized caveolins form the caveolae. The presence of caveolin leads to a local change in morphology of the membrane. [6]
Caveolar endocytosis
Caveolae are one source of clathrin-independent raft-dependent endocytosis. The ability of caveolins to oligomerize due to their oligomerization domains is necessary for formation of caveolar endocytic vesicles. The oligomerization leads to formation of caveolin-rich microdomains in the plasma membrane. Increased levels of cholesterol and insertion of scaffolding domain of caveolins to the plasma membrane then lead to expansion of the caveolar invagination and to formation of endocytic vesicle. Fission of the vesicle from the plasma membrane is then mediated by GTPase dynamin II which is localized at the neck of the budding vesicle. The released caveolar vesicle can fuse with early endosome or caveosome. The caveosome is an endosomal compartment with neutral pH which does not have early endosomal markers, however, contains molecules internalized by the caveolar endocytosis. [6] [7]
This type of endocytosis is used for example for transcytosis of albumin in endothelial cells or for internalization of the insulin receptor in primary adipocytes. [6]
Other roles of caveolae
- Caveolae can be used for entry to the cell by some pathogens and so they avoid degradation in lysosomes. However, some bacteria do not use typical caveolae but only caveolin-rich areas of the plasma membrane. The pathogens exploiting this endocytic pathway include viruses such as SV40 and polyoma virus and bacteria such as some strains of Escherichia coli, Pseudomonas aeruginosa and Porphyromonas gingivalis. [7]
- Caveolae have a role in the cell signaling, too. Caveolins associate with some signaling molecules (e.g. eNOS) through their scaffolding domain and so they can regulate their signaling. Caveolae are also involved in regulation of channels and in calcium signaling. [7]
- Caveolae also participate in lipid regulation. High levels of caveolin Cav1 are expressed in adipocytes. Caveolin associates with cholesterol, fatty acids and lipid droplets and is involved in its regulation. [7]
- Caveolae can also serve as mechanosensors in various cell types. In endothelial cells, caveolae are involved in flow sensation. Chronic exposure to the flow stimulus leads to increased levels of caveolin Cav1 in plasma membrane, its phosphorylation, activation of eNOS signaling enzyme and to remodeling of blood vessels. In smooth-muscle cells, caveolin Cav1 has a role in stretch sensing which triggers cell-cycle progression. [7]
Inhibitors
Some known inhibitors of the caveolae pathway are Filipin III, Genistein and Nystatin. [6]
See also
References
- ^ Anderson RG (1998). "The caveolae membrane system". Annu. Rev. Biochem. 67: 199–225. doi:10.1146/annurev.biochem.67.1.199. PMID 9759488.
- ^ Frank P, Lisanti M (2004). "Caveolin-1 and caveolae in atherosclerosis: differential roles in fatty streak formation and neointimal hyperplasia". Current Opinion in Lipidology 15 (5): 523–9. doi:10.1097/00041433-200410000-00005. PMID 15361787.
- ^ Li X, Everson W, Smart E (2005). "Caveolae, lipid rafts, and vascular disease". Trends Cardiovasc Med 15 (3): 92–6. doi:10.1016/j.tcm.2005.04.001. PMID 16039968.
- ^ Pelkmans L (2005). "Secrets of caveolae- and lipid raft-mediated endocytosis revealed by mammalian viruses". Biochim Biophys Acta 1746 (3): 295–304. doi:10.1016/j.bbamcr.2005.06.009. PMID 16126288.
- ^ Caveolae at the US National Library of Medicine Medical Subject Headings (MeSH)
- ^ a b c d Lajoie, P. and I.R. Nabi, Lipid rafts, caveolae, and their endocytosis. Int Rev Cell Mol Biol, 2010. 282: p. 135-63.
- ^ a b c d e Parton, R.G. and K. Simons, The multiple faces of caveolae. Nature Reviews Molecular Cell Biology, 2007. 8(3): p. 185-94.
External links
- Histology image: 21402loa – Histology Learning System at Boston University
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Structures of the cell membrane
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| Membrane lipids |
- Lipid bilayer
- Phospholipids
- Proteolipids
- Sphingolipids
- Sterols
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| Membrane proteins |
- Membrane glycoproteins
- Integral membrane proteins/transmembrane protein
- Peripheral membrane protein/Lipid-anchored protein
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| Other |
- Caveolae/Coated pits
- Cell junctions
- Glycocalyx
- Lipid raft/microdomains
- Membrane contact sites
- Membrane nanotubes
- Myelin sheath
- Nodes of Ranvier
- Nuclear envelope
- Phycobilisomes
- Porosomes
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Index of cells
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| Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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| Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
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English Journal
- DMSO Enhances TGF-β Activity by Recruiting the Type II TGF-β Receptor From Intracellular Vesicles to the Plasma Membrane.
- Huang SS1, Chen CL2, Huang FW3, Hou WH4, Huang JS4.
- Journal of cellular biochemistry.J Cell Biochem.2016 Jul;117(7):1568-79. doi: 10.1002/jcb.25448. Epub 2016 Feb 18.
- Dimethyl sulfoxide (DMSO) is used to treat many diseases/symptoms. The molecular basis of the pharmacological actions of DMSO has been unclear. We hypothesized that DMSO exerts some of these actions by enhancing TGF-β activity. Here we show that DMSO enhances TGF-β activity by ∼3-4-fold in Mv1Lu
- PMID 26587792
- Nanoscale analysis reveals agonist-sensitive and heterogeneous pools of phosphatidylinositol 4-phosphate in the plasma membrane.
- Yoshida A1, Shigekuni M1, Tanabe K2, Fujita A3.
- Biochimica et biophysica acta.Biochim Biophys Acta.2016 Jun;1858(6):1298-305. doi: 10.1016/j.bbamem.2016.03.011. Epub 2016 Mar 10.
- Phosphatidylinositol 4-phosphate [PtdIns(4)P] is the immediate precursor of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2], which is localized to the cytoplasmic leaflet of the plasma membrane and has been reported to possess multiple cell biological functions. Direct evidence showing the dis
- PMID 26972044
- On the interaction of alginate-based core-shell nanocarriers with keratinocytes in vitro.
- Nguyen HT1, Allard-Vannier E1, Gaillard C2, Eddaoudi I1, Miloudi L1, Soucé M1, Chourpa I1, Munnier E3.
- Colloids and surfaces. B, Biointerfaces.Colloids Surf B Biointerfaces.2016 Jun 1;142:272-80. doi: 10.1016/j.colsurfb.2016.02.055. Epub 2016 Feb 27.
- Calcium alginate nanocarriers (CaANCs) were developed as a potential tool for delivery of hydrophobic active molecules such as pharmaceutical and cosmetic active ingredients. In this study, we focused on interactions between CaANCs and keratinocytes in culture and examined toxicity, internalization
- PMID 26962764
Japanese Journal
- Exosomes Derived from Epstein-Barr Virus-Infected Cells Are Internalized via Caveola-Dependent Endocytosis and Promote Phenotypic Modulation in Target Cells
- Nanbo Asuka,Kawanishi Eri,Yoshida Ryuji,Yoshiyama Hironori
- Journal of virology 87(18), 10334-10347, 2013-09
- … Taken together, our data indicate that exosomes released from EBV-infected B cells are internalized via caveola-dependent endocytosis, which, in turn, contributes to phenotypic changes in the recipient cells through transferring one or more viral factors. …
- NAID 120005372319
- Non-Genomic Regulation of K+ and Ca2+ Channels by Sex Hormones
- Furukawa Tetsushi,Kurokawa Junko,Asada Ken,Bai Chang-Xi,Nakamura Hiroaki,Isobe Mitsuaki,E. Clancy Colleen
- Journal of Arrhythmia 27(Supplement), SS2_1, 2011
- … The non-genomic generation of NO occurred in a signal pathway localized in lipid raft/caveola. …
- NAID 130002130108
Related Links
- caveola [ka″ve-o´lah] (pl. caveo´lae) (L.) one of the minute pits or incuppings of the cell membrane formed during pinocytosis. caveola (kăv-ē-ō′lă) plural.caveolae A small pit or depression formed on the cell surface during pinocytosis.
- caveola [ka″ve-o´lah] (pl. caveo´lae) (L.) one of the minute pits or incuppings of the cell membrane formed during pinocytosis. cav·e·o·la, pl. cav·e·o·lae (kav'ē-ō'lă, -lē), Avoid the mispronunciation caveo'la. A small pocket, vesicle, cave ...
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