Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively
Articolo
Data di Pubblicazione:
2010
Citazione:
Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively / A. Bigi. L. Morosi, C. Pozzi, M. Forcella, G. Tettamanti, B. Venerando, E. Monti, P. Fusi. - In: GLYCOBIOLOGY. - ISSN 0959-6658. - 20:2(2010), pp. cwp156.148-cwp156.157.
Abstract:
Sialidases are widely distributed glycohydrolytic enzymes removing sialic acid residues from glycoconjugates. In mammals, several sialidases with different subcellular localizations and biochemical features have been described. NEU4, the most recently identified member of the human sialidase family, is found in two forms, NEU4 long and NEU4 short, differing in the presence of a 12-amino-acid sequence at the N-terminus. Contradictory data are present in the literature about the subcellular distribution of these enzymes, their membrane anchoring mechanism being still unclear. In this work, we investigate the human NEU4 long and NEU4 short membrane anchoring mechanism and their subcellular localization. Protein extraction with Triton X-114 and sodium carbonate and cross-linking experiments demonstrate that both forms of NEU4 are extrinsic membrane proteins, anchored via protein-protein interactions. Moreover, through confocal microscopy and subcellular fractionation, we show that the long form localizes in mitochondria, while the short form is also associated with the endoplasmic reticulum. Finally, mitochondria subfractionation experiments suggest that NEU4 long is bound to the outer mitochondrial membrane
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
endoplasmic reticulum ; long and short isoforms ; mitochondrial membrane ; peripheral membrane protein ; sialidase NEU4
Elenco autori:
A. Bigi. L. Morosi, C. Pozzi, M. Forcella, G. Tettamanti, B. Venerando, E. Monti, P. Fusi
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