2012
DOI: 10.1016/j.bbamem.2011.10.009
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Selective and programmed cleavage of GPI-anchored proteins from the surface membrane by phospholipase C

Abstract: Many surface proteins of eukaryotic cells are tethered to the membrane by a GPI-anchor which is enzymatically cleavable. Here, we investigate cleavage and release of different GPI-proteins by phospholipase C from the outer membrane of the ciliate Paramecium tetraurelia. Our data indicate that different GPI-proteins are not equally cleaved as proteins of the surface antigen family are preferentially released in vitro compared to several smaller GPI-proteins. Likewise, the analysis of culture medium indicates ex… Show more

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Cited by 35 publications
(24 citation statements)
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“…The ankyrin domain is considered to be the most common location for protein–protein interactions [47] and can play a role in several cellular functions. TisoTranscripts-59 was identified as a GPI protein-like, a category of proteins known for their roles in communication between cells [48]. Given their putative functions, a potential implication of these latter two genes in the lipid over-accumulation observed in Tiso-S2M2 is not obvious, but they should be kept in mind for further studies.…”
Section: Discussionmentioning
confidence: 99%
“…The ankyrin domain is considered to be the most common location for protein–protein interactions [47] and can play a role in several cellular functions. TisoTranscripts-59 was identified as a GPI protein-like, a category of proteins known for their roles in communication between cells [48]. Given their putative functions, a potential implication of these latter two genes in the lipid over-accumulation observed in Tiso-S2M2 is not obvious, but they should be kept in mind for further studies.…”
Section: Discussionmentioning
confidence: 99%
“…), only two appear GPI‐specific—a situation which is even less clear in mammals (Müller et al. ; Staudt et al. ).…”
Section: Specific Conservation and Changes During Evolutionmentioning
confidence: 99%
“…The GPI anchor of proteins can be released by specific phospholipase C (PL-C) forms. From bacterial precursors and from a small number of PL-C paralogs (Leondaritis et al 2011), only two appear GPI-specific-a situation which is even less clear in mammals (M€ uller et al 2012;Staudt et al 2016). GPI proteins accompany evolution of Mono-and Bikonta from low levels on.…”
Section: Gpi-anchored Variant Surface Antigens (Vsags)mentioning
confidence: 99%
“…Finally, a functionality unique to GPI-anchored proteins in lower and higher eukaryotes is that they can be released from the cell surface by cleavage of the lipid anchor by phosphatidylinositol-specific endogenous hydrolases (11) . Such phospholipases show specificity for specific GPI-APs (12) , for example, phospholipase C acts on acetylcholinesterase (13) and phospholipase D on alkaline phosphatase (14) . By controlling the release of GPI-APs from the membrane, these enzymes play a critical regulatory role in their expression and function (15) .…”
Section: Overview Of Protein Lipidationmentioning
confidence: 99%