2021
DOI: 10.1016/j.tcb.2020.11.004
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Dynamic Plasma Membrane Organization: A Complex Symphony

Abstract: Membrane protein organization is essential for proper cellular functioning and the result of a dynamic exchange between protein monomers, nanoscale protein clusters, and microscale higher-order structures. This exchange is affected by both lipid bilayer intrinsic factors, such as lipid rafts and tetraspanins, and extrinsic factors, such as cortical actin and galectins. Because membrane organizers act jointly like instruments in a symphony, it is challenging to define the 'key' organizers. Here, we posit, for t… Show more

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Cited by 67 publications
(47 citation statements)
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“…Tetraspanins are a superfamily of proteins with four transmembrane domains, two extracellular regions and intracellular N-and C-termini (Figure 1) that appear to be present in most multicellular organisms. They function by interacting with specific partner proteins and regulating their intracellular trafficking, lateral mobility, and clustering at the cell surface [33]. There are 33 human tetraspanins, systematically named Tspan1-Tspan33, although cluster of differentiation (CD) nomenclature is more commonly used for those with CD names.…”
Section: Tetraspanin Overviewmentioning
confidence: 99%
“…Tetraspanins are a superfamily of proteins with four transmembrane domains, two extracellular regions and intracellular N-and C-termini (Figure 1) that appear to be present in most multicellular organisms. They function by interacting with specific partner proteins and regulating their intracellular trafficking, lateral mobility, and clustering at the cell surface [33]. There are 33 human tetraspanins, systematically named Tspan1-Tspan33, although cluster of differentiation (CD) nomenclature is more commonly used for those with CD names.…”
Section: Tetraspanin Overviewmentioning
confidence: 99%
“…As indicated above, integrins are included in tetraspanin-enriched microdomains where they can associate with CD36 and VEGFR-2 in a TSP-1-dependent manner. The αv, α5, β1, and β2 integrins have been reported to be present in these complexes (Hemler, 2014;van Deventer et al, 2020).…”
Section: Integrin Binding To Tsp-1mentioning
confidence: 97%
“…CD36 has been reported to be enriched in lipid rafts and tetraspaninenriched microdomains (Miao et al, 2001;Thorne et al, 2006). The tetraspanins are a family of proteins that contain four transmembrane domains (Hemler, 2014;van Deventer et al, 2020). They undergo homo-and heterotypic association to form distinct regions in the plasma membrane that are enriched in integrins and other membrane proteins.…”
Section: Cd36 As a Receptor For Tsp-1mentioning
confidence: 99%
“…Despite lack of extracellular ligands or classical domains/motifs for intracellular protein-protein interactions, tetraspanins are capable of carrying out a variety of functional and signaling roles through at least three distinct types of molecular interactions: (1) Imposing a lateral impact on the activation of their cell surface partners; (2) Recruiting signaling molecules via self-association-based micro- or nano-domains; (3) Long-range impact via regulation of secretory vesicles [ 73 , 102 , 103 , 104 , 105 ]. To date, there is a consensus that tetraspanin molecules, together with their molecular partners, form a nano-scale protein complex or molecular network on the plasma membrane, termed as tetraspanin-enriched microdomain (TEM) [ 3 , 8 , 10 , 102 , 106 ].…”
Section: Molecular Basis For Functional and Signaling Versatility Of Cd151 And Other Tetraspaninsmentioning
confidence: 99%