Abstract
Eukaryotic cell membranes are organized into functional lipid and protein domains, the most widely studied being membrane rafts. They are enriched in sphingolipids and cholesterol and contain several types of membrane proteins such as stomatin and flotillins, which are their “permanent” residents, along with several others, such as receptors, including growth factor receptors.
Membrane rafts in the mature erythrocyte are not the remnants from erythroid precursor cell(s), but are real and dynamic domains functioning within the membrane, helping to fulfil physiological roles, of which only a few of them are just now being recognized.
The important question is the presence and role of the MPP1 protein in these domains in erythroid cells. It was well known that this was a major palmitoylation target in erythrocytes. Here we review data indicating that (palmitoylated) MPP1 functions as an organizer of membrane rafts in erythroid cells. This conclusion is strengthened by the fact that a lack of MPP1 palmitoylation, resulting from an absence of DHHC17, the only erythroid palmitoyltransferase, leads to the unique pathology of human organism.
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- a ZO1:
-
A mammalian zonula occludens protein
- DlgA:
-
A Drosophila disc large tumor suppressor
- DRM:
-
Detergent resistant membrane
- FLIM Fluorescence lifetime imaging L27:
-
Lin-2 and Lin-7 receptor targeting proteins
- ld:
-
Liquid disordered
- lo:
-
Liquid ordered
- MAGUK:
-
Membrane associated guanylate kinase
- MPP1:
-
Membrane palmitoylated protein-1
- PC:
-
Phosphatidylcholine
- PDZ PSD:
-
Post synaptic density protein
- PE:
-
Phosphatidylethanolamine
- PS:
-
Phosphatidylserine
- SH3:
-
Src homology 3 domain
- SM:
-
Sphingomyelin
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Sikorski, A.F., Podkalicka, J., Jones, W., Biernatowska, A. (2015). Membrane Rafts in the Erythrocyte Membrane: A Novel Role of MPP1p55. In: Chakrabarti, A., Surolia, A. (eds) Biochemical Roles of Eukaryotic Cell Surface Macromolecules. Advances in Experimental Medicine and Biology, vol 842. Springer, Cham. https://doi.org/10.1007/978-3-319-11280-0_5
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