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Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly

Mayerhofer, PU, Kattenfeld, T, Roscher, AA and Muntau, AC (2002) Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly Biochem Biophys Res Commun, 291. pp. 1180-1186.

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Abstract

PEX19 has been shown to play a central role in the early steps of peroxisomal membrane synthesis. Computational database analysis of the PEX19 sequence revealed three different conserved domains: D1 (aa 1--87), D2 (aa 88--272), and D3 (aa 273--299). However, these domains have not yet been linked to specific biological functions. We elected to functionally characterize the proteins derived from two naturally occurring PEX19 splice variants: PEX19DeltaE2 lacking the N-terminal domain D1 and PEX19DeltaE8 lacking the domain D3. Both interact with peroxisomal ABC transporters (ALDP, ALDRP, PMP70) and with full-length PEX3 as shown by in vitro protein interaction studies. PEX19DeltaE8 also interacts with a PEX3 protein lacking the peroxisomal targeting region located at the N-terminus (Delta66aaPEX3), whereas PEX19DeltaE2 does not. Functional complementation studies in PEX19-deficient human fibroblasts revealed that transfection of PEX19DeltaE8-cDNA leads to restoration of both peroxisomal membranes and of functional peroxisomes, whereas transfection of PEX19DeltaE2-cDNA does not restore peroxisomal biogenesis. Human PEX19 is partly farnesylated in vitro and in vivo. The farnesylation consensus motif CLIM is located in the PEX19 domain D3. The finding that the protein derived from the splice variant lacking D3 is able to interact with several peroxisomal membrane proteins and to restore peroxisomal biogenesis challenges the previous assumption that farnesylation of PEX19 is essential for its biological functionality. The data presented demonstrate a considerable functional diversity of the proteins encoded by two PEX19 splice variants and thereby provide first experimental evidence for specific biological functions of the different predicted domains of the PEX19 protein.

Item Type: Article
Authors :
NameEmailORCID
Mayerhofer, PUp.mayerhofer@surrey.ac.ukUNSPECIFIED
Kattenfeld, TUNSPECIFIEDUNSPECIFIED
Roscher, AAUNSPECIFIEDUNSPECIFIED
Muntau, ACUNSPECIFIEDUNSPECIFIED
Date : 2002
Identification Number : 10.1006/bbrc.2002.6568
Uncontrolled Keywords : Alternative Splicing Animals COS Cells Cercopithecus aethiops Genetic Complementation Test Humans Membrane Proteins/chemistry/genetics/*physiology Peroxisomes/*physiology Protein Isoforms/physiology Protein Structure, Tertiary
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:42
Last Modified : 17 May 2017 14:51
URI: http://epubs.surrey.ac.uk/id/eprint/828855

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