the Pex1p/Pex6p complex exhibits a dual localization, with one fraction anchored to the peroxisomal membrane by its interaction to Pex15p and the second fraction located in the cytosol
the Pex1p/Pex6p-complex shows a dual localization in the cell as it is located in the cytosol as well as at the peroxisomal membrane. Association of this complex with the peroxisomal membrane is mediated by binding to Pex15p. The predominant part of the tail anchored protein Pex15p faces the cytosol and mediates the peroxisomal membrane association of the AAA-complex via a direct interaction with the N-terminal domain of Pex6p, assembly of the Pex1p/Pex6p-complex and recruitment to the peroxisomal membrane
the Pex1p/Pex6p-complex shows a dual localization in the cell as it is located in the cytosol as well as at the peroxisomal membrane. Association of this complex with the peroxisomal membrane is mediated by binding to Pex15p. The predominant part of the tail-anchored protein Pex15p faces the cytosol and mediates the peroxisomal membrane association of the AAA-complex via a direct interaction with the N-terminal domain of Pex6p, assembly of the Pex1p/Pex6p-complex and recruitment to the peroxisomal membrane
the Pex1p/Pex6p complex exhibits a dual localization, with one fraction anchored to the peroxisomal membrane by its interaction to Pex15p and the second fraction located in the cytosol
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1pPex6p complex to the membrane
the tail-anchored protein Pex26p in humans functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex26p and mediates the attachment of the Pex1pPex6p complex to the membrane
the AAAdomains of Pex6p seem to influence the Pex6p/Pex15p-interaction and thereby regulate the recruitment of the cytosolic AAA-complex to the peroxisomal membrane, although in opposite fashion. In particular, ATP-binding to D1 of Pex6p stimulates association of the AAA-complex with Pex15p at the peroxisomal membrane while ATP-hydrolysis at D2 seems to trigger the release of the AAA-complex from Pex15p and thus from the membrane
the AAAdomains of Pex6p seem to influence the Pex6p/Pex15p-interaction and thereby regulate the recruitment of the cytosolic AAA-complex to the peroxisomal membrane, although in opposite fashion. In particular, ATP-binding to D1 of Pex6p stimulates association of the AAA-complex with Pex15p at the peroxisomal membrane while ATP-hydrolysis at D2 seems to trigger the release of the AAA-complex from Pex15p and thus from the membrane
the tail-anchored protein Pex15p in yeast functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex15p and mediates the attachment of the Pex1p-Pex6p complex to the membrane
the tail-anchored protein Pex15p in yeast functions as membrane anchors responsible for the recruitment of the Pex1p-Pex6p complex to the peroxisomal membrane, the N-terminal domain of Pex6p interacts with the cytosolic part of Pex15p and mediates the attachment of the Pex1p-Pex6p complex to the membrane