The Pex3–Inp1 complex tethers yeast peroxisomes to the plasma membrane
| Autor: | James M. Nuttall, Ellen G. Allwood, Georgia E. Hulmes, John D Hutchinson, Kathryn R. Ayscough, Noa Dahan, Ewald H. Hettema |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Peroxisomal membrane Saccharomyces cerevisiae Biology Phosphatidylinositols Biochemistry Microbiology Cell membrane Peroxins Report Cell cortex Pi medicine Peroxisomes Amino Acid Sequence Organelles Membrane and Lipid Biology Cell Membrane Membrane Proteins Cell Biology Peroxisome Yeast Cell biology Membrane medicine.anatomical_structure Multiprotein Complexes Protein Binding |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Organelle inheritance in yeast is a balance between two opposing processes, retention and inheritance. Hulmes et al. propose a new model for peroxisome retention involving contact with the plasma membrane and identify the plasma membrane–peroxisome tether responsible. A subset of peroxisomes is retained at the mother cell cortex by the Pex3–Inp1 complex. We identify Inp1 as the first known plasma membrane–peroxisome (PM-PER) tether by demonstrating that Inp1 meets the predefined criteria that a contact site tether protein must adhere to. We show that Inp1 is present in the correct subcellular location to interact with both the plasma membrane and peroxisomal membrane and has the structural and functional capacity to be a PM-PER tether. Additionally, expression of artificial PM-PER tethers is sufficient to restore retention in inp1Δ cells. We show that Inp1 mediates peroxisome retention via an N-terminal domain that binds PI(4,5)P2 and a C-terminal Pex3-binding domain, forming a bridge between the peroxisomal membrane and the plasma membrane. We provide the first molecular characterization of the PM-PER tether and show it anchors peroxisomes at the mother cell cortex, suggesting a new model for peroxisome retention. |
| Databáze: | OpenAIRE |
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