Identification of the site of attachment of the glycolipid anchor in porcine membrane dipeptidase

Brewis, Ian Andrew, Hooper, N. M. and Turner, A. J. 1993. Identification of the site of attachment of the glycolipid anchor in porcine membrane dipeptidase. Biochemical Society Transactions 21 , 44S-44S. 10.1042/bst021044s

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Abstract

A significant number of cell-surface proteins m anchored in the plasma membrane by covalently attached glycosyl-phosphatidylinositol(glycolipid) and to date over 100 examples have been described from many stages of eukaryotic evolution [reviewed in 131. As well as having an N-terminal signal sequence to direct the protein to the ER, glycolipid-anchored proteins also have encoded in their cDNA a C-terminal hydrophobic region of amino acids. This sequence is believed to hold the nascent protein in the membrane prior to anchor addition and is cleaved off posttranslationally with concomitant addition of the glycolipid anchor. Anchor attachment occurs on the terminal residue present after cleavage which may be one of six small side-chain residues (Ala, Asn, Asp, Cys, Gly or, most commonly, Ser) [ 11. It has also recently been shown that a depe of specificity, again for small amino acids, exists in the two adjacent C-terminal amino acid positions, in particular the residue next but one to the attachment residue may only be Ala, Gly or Ser [3]. Here we report the determination of the site of glycolipid anchor attachment of porcine membrane dipeptidase(dehydropeptidase-I; EC3.4.13.11).

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Subjects:	R Medicine > R Medicine (General)
Publisher:	Portland Press
ISSN:	0300-5127
Last Modified:	04 Jun 2017 06:13
URI:	https://orca.cardiff.ac.uk/id/eprint/57435

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