scholarly journals Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation

FEBS Journal ◽  
2019 ◽  
Vol 287 (9) ◽  
pp. 1742-1757 ◽  
Author(s):  
Ritika Singh ◽  
Selvambigai Manivannan ◽  
Arjen M. Krikken ◽  
Rinse Boer ◽  
Nicola Bordin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Hansenula Polymorpha ◽  
Peroxisomal Membrane ◽  
Peroxisomal Membrane Protein

scholarly journals Pex24 and Pex32 tether peroxisomes to the ER for organelle biogenesis, positioning and segregation

2020 ◽  
Author(s):  
Fei Wu ◽  
Rinse de Boer ◽  
Arjen M. Krikken ◽  
Arman Akşit ◽  
Nicola Bordin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Hansenula Polymorpha ◽  
Peroxisome Biogenesis ◽  
Organelle Biogenesis ◽  
Peroxisomal Membrane ◽  
Peroxisomal Protein ◽  
Peroxisomal Membrane Protein ◽  
Contact Formation ◽  
And Function

AbstractWe analyzed all four Pex23 family proteins of the yeast Hansenula polymorpha, which localize to the ER. Of these Pex24 and Pex32, but not Pex23 and Pex29, accumulate at peroxisome-ER contacts, where they are important for normal peroxisome biogenesis and proliferation and contribute to organelle positioning and segregation.Upon deletion of PEX24 and PEX32 - and to a lesser extent of PEX23 and PEX29 - peroxisome-ER contacts are disrupted, concomitant with peroxisomal defects. These defects are suppressed upon introduction of an artificial peroxisome-ER tether.Accumulation of Pex32 at peroxisomes-ER contacts is lost in the absence of the peroxisomal membrane protein Pex11. At the same time peroxisome-ER contacts are disrupted, indicating that Pex11 contributes to Pex32-dependent peroxisome-ER contact formation.Summarizing, our data indicate that H. polymorpha Pex24 and Pex32 are tethers at peroxisome-ER contacts that are important for normal peroxisome biogenesis and dynamics.SummaryTwo Hansenula polymorpha ER proteins, Pex24 and Pex32, are tethers at peroxisome-ER contacts and function together with the peroxisomal protein Pex11. Their absence disturbs these contacts leading to multiple peroxisomal defects, which can be restored by an artificial tether.

scholarly journals Hydrophobic Regions Adjacent to Transmembrane Domains 1 and 5 Are Important for the Targeting of the 70-kDa Peroxisomal Membrane Protein

2007 ◽  
Vol 282 (46) ◽  
pp. 33831-33844 ◽  
Author(s):  
Yoshinori Kashiwayama ◽  
Kota Asahina ◽  
Masashi Morita ◽  
Tsuneo Imanaka
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Protein Targeting ◽  
Fluorescent Protein ◽  
Chinese Hamster Ovary Cells ◽  
Intracellular Localization ◽  
Chinese Hamster ◽  
Transmembrane Domains ◽  
Peroxisomal Membrane ◽  
Peroxisomal Membrane Protein

The 70-kDa peroxisomal membrane protein (PMP70) is a major component of peroxisomal membranes. Human PMP70 consists of 659 amino acid residues and has six putative transmembrane domains (TMDs). PMP70 is synthesized on cytoplasmic ribosomes and targeted posttranslationally to peroxisomes by an unidentified peroxisomal membrane protein targeting signal (mPTS). In this study, to examine the mPTS within PMP70 precisely, we expressed various COOH-terminally or NH2-terminally deleted constructs of PMP70 fused with green fluorescent protein (GFP) in Chinese hamster ovary cells and determined their intracellular localization by immunofluorescence. In the COOH-terminally truncated PMP70, PMP70(AA.1-144)-GFP, including TMD1 and TMD2 of PMP70, was still localized to peroxisomes. However, by further removal of TMD2, PMP70(AA.1-124)-GFP lost the targeting ability, and PMP70(TMD2)-GFP did not target to peroxisomes by itself. The substitution of TMD2 in PMP70(AA.1-144)-GFP for TMD4 or TMD6 did not affect the peroxisomal localization, suggesting that PMP70(AA.1-124) contains the mPTS and an additional TMD is required for the insertion into the peroxisomal membrane. In the NH2-terminal 124-amino acid region, PMP70 possesses hydrophobic segments in the region adjacent to TMD1. By the disruption of these hydrophobic motifs by the mutation of L21Q/L22Q/L23Q or I70N/L71Q, PMP70(AA.1-144)-GFP lost targeting efficiency. The NH2-terminally truncated PMP70, GFP-PMP70(AA.263-375), including TMD5 and TMD6, exhibited the peroxisomal localization. PMP70(AA.263-375) also possesses hydrophobic residues (Ile307/Leu308) in the region adjacent to TMD5, which were important for targeting. These results suggest that PMP70 possesses two distinct targeting signals, and hydrophobic regions adjacent to the first TMD of each region are important for targeting.

scholarly journals Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p

2010 ◽  
Vol 29 (24) ◽  
pp. 4083-4093 ◽  
Author(s):  
Yasuhiko Sato ◽  
Hiroyuki Shibata ◽  
Toru Nakatsu ◽  
Hiroaki Nakano ◽  
Yoshinori Kashiwayama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Peroxisomal Membrane ◽  
Protein Carrier ◽  
Peroxisomal Membrane Protein

scholarly journals Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Leonidas Emmanouilidis ◽  
Ulrike Schütz ◽  
Konstantinos Tripsianes ◽  
Tobias Madl ◽  
Juliane Radke ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Allosteric Modulation ◽  
Protein Recognition ◽  
Peroxisomal Membrane ◽  
Peroxisomal Membrane Protein ◽  
Import Receptor
Sign in / Sign up

Export Citation Format

Share Document