Search results for PEX3

Showing 16 results out of 19

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Protein (2 results from a total of 2)

Identifier: R-HSA-382608
Species: Homo sapiens
Compartment: peroxisomal membrane
Primary external reference: UniProt: PEX3: P56589
Identifier: R-HSA-9603792
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PEX3: P56589

Reaction (6 results from a total of 9)

Identifier: R-HSA-9603801
Species: Homo sapiens
Compartment: cytosol
In the cytosol, PEX19 binds to newly translated PEX3 (inferred from human PEX19 binding rat Pex3). PEX19 binds the C-terminal region of PEX3 and the membrane targeting signal of PEX3 is located in the N-terminal region (Soukupova et al. 1999, Fransen et al. 2001, Fransen et al. 2005).
Identifier: R-NUL-9604093
Species: Rattus norvegicus, Homo sapiens
Compartment: cytosol
In the cytosol, human PEX19 binds to newly translated rat Pex3 (Matsuzaki and Fujiki 2008).
Identifier: R-HSA-9603784
Species: Homo sapiens
Compartment: peroxisomal membrane
Cytosolic PEX19 bound to a peroxisomal membrane protein binds PEX3 which is located in the peroxisomal membrane and serves as a docking receptor for PEX19 (Soukupova et al. 1999, Muntau et al. 2003, Fang et al. 2004, Matsuzono and Fujiki 2006, Matsuzono et al. 2006, Pinto et al. 2006, Sato et al. 2008, Sato et al. 2010, Schmidt et al. 2010, Hattula et al. 2014, reviewed in Fujiki et al. 2006). PEX19 bound to a cargo protein has much higher affinity for PEX3 than PEX19 alone does (Pinto et al. 2006). The insertion of the peroxisomal membrane protein into the membrane does not require ATP hydrolysis or GTP hydrolysis (Pinto et al. 2006). The N-terminal region of PEX19 binds a hydrophobic groove and acidic cluster on the surface of PEX3 (Schmidt et al. 2010, Schmidt et al. 2012) at the cytosolic apex of the PEX3 spheroid (Sato et al. 2010).
Identifier: R-HSA-9603791
Species: Homo sapiens
Compartment: peroxisomal membrane
The PEX16:PEX19:PEX3 complex dissociates, yielding cytosolic PEX19 and PEX3 and PEX16 inserted in the membrane (inferred from human PEX16, human PEX19, and rat PEX3).
Identifier: R-NUL-9604116
Species: Rattus norvegicus, Homo sapiens
Compartment: peroxisomal membrane
The PEX16:PEX19:Pex3 complex dissociates, yielding cytosolic PEX19 and Pex3 and PEX16 inserted in the membrane (human PEX16, human PEX19, and rat Pex3, Matsuzaki and Fujiki 2008).
Identifier: R-HSA-9603797
Species: Homo sapiens
Compartment: peroxisomal membrane
The cytosolic PEX19:PEX3 complex binds PEX16 located in the peroxisomal membrane (inferred from human PEX19, human PEX16, and rat Pex3). Thus PEX16 serves as a docking factor. PEX3 is believed to be inserted in the peroxisomal membrane by this pathway and by direct co-translational insertion in the membrane of the endoplasmic reticulum that then buds to generate peroxisomes.

Complex (5 results from a total of 5)

Identifier: R-HSA-9603799
Species: Homo sapiens
Compartment: cytosol
Identifier: R-NUL-9604081
Species: Rattus norvegicus, Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9603800
Species: Homo sapiens
Compartment: peroxisomal membrane
Identifier: R-NUL-9604109
Species: Rattus norvegicus, Homo sapiens
Compartment: peroxisomal membrane
Identifier: R-HSA-9603793
Species: Homo sapiens
Compartment: peroxisomal membrane

Pathway (2 results from a total of 2)

Identifier: R-HSA-9603798
Species: Homo sapiens
Most peroxisomal membrane proteins (PMPs) are inserted into the peroxisomal membrane by the receptor-chaperone PEX19 and the docking receptor PEX3 (Soukupova et al. 1999, Muntau et al. 2003, Fang et al. 2004, Fujiki et al. 2006, Matsuzono and Fujiki 2006, Matsuzono et al. 2006, Pinto et al. 2006, Sato et al. 2008, Sato et al. 2010, Schmidt et al. 2010, Hattula et al. 2014, reviewed in Fujiki et al. 2014, Mayerhofer 2016). PEX19 binds the PMP as it is translated in the cytosol. Recognition of the PMP by PEX 19 appears to depend on positively charged residues in the transmembrane domain of the PMP (Costello et al. 2017). The PEX19:PMP complex then interacts with PEX3 located in the peroxisomal membrane. Through a mechanism that is not yet clear, the PMP is inserted into the peroxisomal membrane and PEX19 dissociates from PEX3. A current model involves transfer of the PMP from PEX19 to a hydrophobic region of PEX3 followed by insertion of the PMP into the membrane (Chen et al. 2014, reviewed by Giannopoulou et al. 2016). The process does not appear to require hydrolysis of ATP or GTP (Pinto et al. 2006).
Unlike other PMPs, PEX3 is inserted into the peroxisomal membrane by binding PEX19 and then docking with PEX16 (Matsuzaki and Fujiki 2008). Both PEX3 and PEX16 can also be co-translationally inserted into the endoplasmic reticulum membrane (Kim et al. 2006, Yonekawa et al. 2011, Aranovich et al. 2014, Hua et al. 2015, Mayerhofer et al. 2016). This region of the ER membrane then buds to contribute to new peroxisomes. PEX3 is also observed to insert into the mitochondrial outer membrane (Sugiura et al. 2017). Regions of the ER membrane and mitochondrial outer membrane are then released to form pre-peroxisomal vesicles which fuse to form new peroxisomes (Sugiura et al. 2017). Peroxisomes therefore appear to arise from fission of existing peroxisomes and production of new peroxisomes from precursors derived from mitochondria and the ER (Sugiura et al. 2017, reviewed in Fujiki et al. 2014, Hua and Kim 2016).
Identifier: R-HSA-9609507
Species: Homo sapiens
Protein localization encompasses the processes that establish and maintain proteins at specific locations. Mechanisms that target proteins to particular locations in the cell typically involve a motif in the targeted protein that interacts with proteins located at the destination (reviewed in Bauer et al. 2015).
Mitochondrial proteins encoded in the nucleus may be targeted to the outer membrane, intermembrane space, inner membrane, or the matrix (reviewed in Kutik et al. 2007, Milenkovic et al. 2007, Bolender et al. 2008, Ender and Yamano 2009, Wiedemann and Pfanner 2017, Kang et al. 2018). A presequence or an internal targeting sequence causes a protein in the cytosol to interact with the TOMM40:TOMM70 complex in the outer mitochondrial membrane. After passage across the outer membrane, sequence motifs cause proteins to be targeted to the outer membrane via the SAMM50 complex, to the inner membrane via the TIMM22 or TIMM23 complexes, to the matrix via the TIMM23 complex, or proteins may fold and remain in the intermembrane space.
All of the proteins contained in the peroxisomal matrix are imported from the cytosol by a unique mechanism that does not require the imported proteins to be unfolded as they cross the membrane (reviewed in Ma et al. 2011, Fujiki et al. 2014, Francisco et al. 2017). In the cytosol, receptor proteins, PEX5 and PEX7, bind to specific sequence motifs in cargo proteins and then interact with a protein complex containing PEX13, PEX14, PEX2, PEX10, and PEX12 in the peroxisome membrane. The cargo proteins then pass through a proteinaceous channel in the membrane and PEX5 is recycled by a mechanism involving ubiquitination and deubiquitination.
Most peroxisomal membrane proteins (PMPs) are inserted into the peroxisomal membrane by the receptor-chaperone PEX19 and the docking receptor PEX3 (reviewed in Ma et al. 2011, Fujiki et al. 2014). PEX19 binds the PMP as it is translated in the cytosol. The PEX19:PMP complex then interacts with PEX3 located in the peroxisomal membrane. Through a mechanism that is not yet clear, the PMP is inserted into the peroxisomal membrane and PEX19 dissociates from PEX3.

Icon (1 results from a total of 1)

Species: Homo sapiens
Curator: Bruce May
Designer: Cristoffer Sevilla
PEX3 icon
Peroxisomal biogenesis factor 3
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