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Reggie/flotillin and the targeted delivery of cargo
Author(s) -
Stuermer Claudia A. O.
Publication year - 2011
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2010.07007.x
Subject(s) - microbiology and biotechnology , intracellular , membrane protein , cell membrane , biology , cell surface receptor , signal transduction , cell , lipid microdomain , receptor , chemistry , membrane , biochemistry
J. Neurochem. (2011) 116 , 708–713. Abstract The two proteins reggie‐1/flotillin‐2 and reggie‐2/flotillin‐1 form microdomains at the plasma membrane and at intracellular compartments where src tyrosine kinases associate with them. Specific GPI‐anchored proteins, in particular prion protein and Thy‐1, co‐cluster with reggie microdomains at the plasma membrane and elicit signal transduction in association with reggies which regulates the activation of several GTPases involved in the recruitment of specific membrane proteins from intracellular carriers to target sites of the cell membrane in a cell type‐specific manner. For example, prion protein and reggie regulate the recruitment and targeted delivery of the T cell receptor complex to the T cell cap, of E‐cadherin to cell–cell contact sites in epithelial cells, and of bulk membrane and growth receptors to the growth cone in developing neurons. Evidence is accumulating that reggies are involved in guiding the cell‐type‐specific membrane proteins from the intracellular compartments to their target sites at the cell membrane, a function required in all cells which explains why reggies are expressed in many or all cells in invertebrates and vertebrates.