PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins

Yi Fang, James C. Morrell, Jacob M. Jones, Stephen J Gould

Research output: Contribution to journalArticle

Abstract

PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19.

Original languageEnglish (US)
Pages (from-to)863-875
Number of pages13
JournalJournal of Cell Biology
Volume164
Issue number6
DOIs
StatePublished - Mar 15 2004

Fingerprint

Peroxisomes
Membrane Proteins
Membranes
Organelles
Cytoplasm
Proteins

Keywords

  • Organelle biogenesis
  • PMP import
  • Protein import
  • Temperature-sensitive mutants
  • Zellweger syndrome

ASJC Scopus subject areas

  • Cell Biology

Cite this

PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. / Fang, Yi; Morrell, James C.; Jones, Jacob M.; Gould, Stephen J.

In: Journal of Cell Biology, Vol. 164, No. 6, 15.03.2004, p. 863-875.

Research output: Contribution to journalArticle

Fang, Yi ; Morrell, James C. ; Jones, Jacob M. ; Gould, Stephen J. / PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. In: Journal of Cell Biology. 2004 ; Vol. 164, No. 6. pp. 863-875.
@article{2835a285060848d9b688b52c167789ed,
title = "PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins",
abstract = "PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19.",
keywords = "Organelle biogenesis, PMP import, Protein import, Temperature-sensitive mutants, Zellweger syndrome",
author = "Yi Fang and Morrell, {James C.} and Jones, {Jacob M.} and Gould, {Stephen J}",
year = "2004",
month = "3",
day = "15",
doi = "10.1083/jcb.200311131",
language = "English (US)",
volume = "164",
pages = "863--875",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "6",

}

TY - JOUR

T1 - PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins

AU - Fang, Yi

AU - Morrell, James C.

AU - Jones, Jacob M.

AU - Gould, Stephen J

PY - 2004/3/15

Y1 - 2004/3/15

N2 - PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19.

AB - PEX19 is a chaperone and import receptor for newly synthesized, class I peroxisomal membrane proteins (PMPs). PEX19 binds these PMPs in the cytoplasm and delivers them to the peroxisome for subsequent insertion into the peroxisome membrane, indicating that there may be a PEX19 docking factor in the peroxisome membrane. Here we show that PEX3 is required for PEX19 to dock at peroxisomes, interacts specifically with the docking domain of PEX19, and is required for recruitment of the PEX19 docking domain to peroxisomes. PEX3 is also sufficient to dock PEX19 at heterologous organelles and binds PEX19 via a conserved motif that is essential for this docking activity and for PEX3 function in general. Not surprisingly, transient inhibition of PEX3 abrogates class I PMP import but has no effect on class II PMP import or peroxisomal matrix protein import. Taken together, these results suggest that PEX3 plays a selective, essential, and direct role in PMP import as a docking factor for PEX19.

KW - Organelle biogenesis

KW - PMP import

KW - Protein import

KW - Temperature-sensitive mutants

KW - Zellweger syndrome

UR - http://www.scopus.com/inward/record.url?scp=1642394134&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1642394134&partnerID=8YFLogxK

U2 - 10.1083/jcb.200311131

DO - 10.1083/jcb.200311131

M3 - Article

C2 - 15007061

AN - SCOPUS:1642394134

VL - 164

SP - 863

EP - 875

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 6

ER -