Search results for SAMM50

Showing 6 results out of 6

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Types

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Protein (1 results from a total of 1)

Identifier: R-HSA-1252178
Species: Homo sapiens
Compartment: mitochondrial outer membrane
Primary external reference: UniProt: SAMM50: Q9Y512

Complex (1 results from a total of 1)

Identifier: R-HSA-1252247
Species: Homo sapiens
Compartment: mitochondrial outer membrane
The SAM complex is inferred from homologous subunits in Saccharomyces cerevisiae. Xie et al. (2007) found human SAM50 in a complex with metaxin 1, metaxin 2, mitofilin, CHCHD3, CHCHD6, and DnaJC1 however Kozjak-Pavlovic et al. (2007) found SAM50 in a separate complex from the metaxins.

Reaction (2 results from a total of 2)

Identifier: R-HSA-1268025
Species: Homo sapiens
Compartment: mitochondrial intermembrane space, mitochondrial outer membrane
As inferred from the yeast SAM50 complex, the human SAMM50 Complex (SAM50 complex, TOB55 complex) inserts mainly beta-barrel proteins into the outer membrane after they have passed from the cytosol, through the TOMM40:TOMM70 complex, and into the intermembrane space.
In yeast, experimentally verified substrates of the SAM50 complex include TOM40 (TOMM40 in human), MDM10, Porin1 (VDAC1 in human), and TOM22 (TOMM22 in human). In humans, TOMM40 (Humphries et al. 2005) and VDAC1 (Kozjak-Pavlovic et al. 2007, homologous to yeast Porin1) have been shown to be substrates. Many other mitochondrial proteins are anticipated to be substrates of the SAMM50 complex.
Identifier: R-HSA-9714477
Species: Homo sapiens
Compartment: mitochondrial outer membrane
RAC2 interacts with several effectors localized at the mitochondrial outer membrane. Since RAC2 localization at the mitochondrial outer membrane and its association with mitochondrial proteins has not been fully established, these effectors are annotated as candidates:
ARMCX3 (Bagci et al. 2020)
MTX1 (Capala et al. 2015)
SAMM50 (Capala et al. 2015)

Pathway (2 results from a total of 2)

Identifier: R-HSA-1268020
Species: Homo sapiens
Compartment: cytosol, mitochondrial inner membrane, mitochondrial intermembrane space, mitochondrial matrix, mitochondrial outer membrane
A human mitochondrion contains about 1500 proteins, more than 99% of which are encoded in the nucleus, synthesized in the cytosol and imported into the mitochondrion. Proteins are targeted to four locations (outer membrane, intermembrane space, inner membrane, and matrix) and must be sorted accordingly (reviewed in Kutik et al. 2007, Milenkovic et al. 2007, Bolender et al. 2008, Endo and Yamano 2009, Wiedemann and Pfanner 2017, Kang et al. 2018). Newly synthesized proteins are transported from the cytosol across the outer membrane by the TOMM40:TOMM70 complex. Proteins that contain presequences first interact with the TOMM20 subunit of the complex while proteins that contain internal targeting elements first interact with the TOMM70 subunit. After initial interaction the protein is conducted across the outer membrane by TOMM40 subunits. In yeast some proteins such as Aco1, Atp1, Cit1, Idh1, and Atp2 have both presequences that interact with TOM20 and mature regions that interact with TOM70 (Yamamoto et al. 2009).
After passage across the outer membrane, proteins may be targeted to the outer membrane via the SAMM50 complex, to the inner membrane via the TIMM22 or TIMM23 complexes (reviewed in van der Laan et al. 2010), to the matrix via the TIMM23 complex (reviewed in van der Laan et al. 2010), or proteins may fold and remain in the intermembrane space (reviewed in Stojanovski et al. 2008, Deponte and Hell 2009, Sideris and Tokatlidis 2010). Presequences on matrix and inner membrane proteins cause interaction with TIMM23 complexes; internal targeting sequences cause outer membrane proteins to interact with the SAMM50 complex and inner membrane proteins to interact with the TIMM22 complex. While in the intermembrane space hydrophobic proteins are chaperoned by the TIMM8:TIMM13 complex and/or the TIMM9:TIMM10:FXC1 complex.
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.
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