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

Standard

Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly. / Mayerhofer, Peter U; Kattenfeld, Tanja; Roscher, Adelbert A; Muntau, Ania C.

in: BIOCHEM BIOPH RES CO, Jahrgang 291, Nr. 5, 15.03.2002, S. 1180-6.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Mayerhofer, PU, Kattenfeld, T, Roscher, AA & Muntau, AC 2002, 'Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly', BIOCHEM BIOPH RES CO, Jg. 291, Nr. 5, S. 1180-6. https://doi.org/10.1006/bbrc.2002.6568

APA

Mayerhofer, P. U., Kattenfeld, T., Roscher, A. A., & Muntau, A. C. (2002). Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly. BIOCHEM BIOPH RES CO, 291(5), 1180-6. https://doi.org/10.1006/bbrc.2002.6568

Vancouver

Mayerhofer PU, Kattenfeld T, Roscher AA, Muntau AC. Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly. BIOCHEM BIOPH RES CO. 2002 Mär 15;291(5):1180-6. https://doi.org/10.1006/bbrc.2002.6568

Bibtex

@article{7e72b74177dc496b87b7876ead6fa961,
title = "Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly",
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.",
keywords = "Alternative Splicing, Animals, COS Cells, Chlorocebus aethiops, Genetic Complementation Test, Humans, Membrane Proteins/chemistry, Peroxisomes/physiology, Protein Isoforms/physiology, Protein Structure, Tertiary",
author = "Mayerhofer, {Peter U} and Tanja Kattenfeld and Roscher, {Adelbert A} and Muntau, {Ania C}",
note = "(C)2002 Elsevier Science (USA).",
year = "2002",
month = mar,
day = "15",
doi = "10.1006/bbrc.2002.6568",
language = "English",
volume = "291",
pages = "1180--6",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly

AU - Mayerhofer, Peter U

AU - Kattenfeld, Tanja

AU - Roscher, Adelbert A

AU - Muntau, Ania C

N1 - (C)2002 Elsevier Science (USA).

PY - 2002/3/15

Y1 - 2002/3/15

N2 - 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.

AB - 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.

KW - Alternative Splicing

KW - Animals

KW - COS Cells

KW - Chlorocebus aethiops

KW - Genetic Complementation Test

KW - Humans

KW - Membrane Proteins/chemistry

KW - Peroxisomes/physiology

KW - Protein Isoforms/physiology

KW - Protein Structure, Tertiary

U2 - 10.1006/bbrc.2002.6568

DO - 10.1006/bbrc.2002.6568

M3 - SCORING: Journal article

C2 - 11883941

VL - 291

SP - 1180

EP - 1186

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 5

ER -