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Human peroxin PEX3 is co-translationally integrated into the ER and exits the ER in budding vesicles

Mayerhofer, PU, Bano-Polo, M, Mingarro, I and Johnson, AE (2015) Human peroxin PEX3 is co-translationally integrated into the ER and exits the ER in budding vesicles Traffic.

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Abstract

The long-standing paradigm that all peroxisomal proteins are imported post-translationally into preexisting peroxisomes has been challenged by the detection of peroxisomal membrane proteins (PMPs) inside the endoplasmic reticulum (ER). In mammals, the mechanisms of ER entry and exit of PMPs are completely unknown. We show that the human PMP PEX3 inserts co-translationally into the mammalian ER via the Sec61 translocon. Photocrosslinking and fluorescence spectroscopy studies demonstrate that the N-terminal transmembrane segment (TMS) of ribosome-bound PEX3 is recognized by the signal recognition particle (SRP). Binding to SRP is a prerequisite for targeting of the PEX3-containing ribosome*nascent chain complex (RNC) to the translocon, where an ordered multistep pathway integrates the nascent chain into the membrane adjacent to translocon proteins Sec61alpha and TRAM. This insertion of PEX3 into the ER is physiologically relevant because PEX3 then exits the ER via budding vesicles in an ATP-dependent process. This study identifies early steps in human peroxisomal biogenesis by demonstrating sequential stages of PMP passage through the mammalian ER.

Item Type: Article
Authors :
NameEmailORCID
Mayerhofer, PUp.mayerhofer@surrey.ac.ukUNSPECIFIED
Bano-Polo, MUNSPECIFIEDUNSPECIFIED
Mingarro, IUNSPECIFIEDUNSPECIFIED
Johnson, AEUNSPECIFIEDUNSPECIFIED
Date : 2015
Identification Number : https://doi.org/10.1111/tra.12350
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/828845

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