Transport activity-dependent intracellular sorting of the yeast general amino acid permease
Intracellular trafficking of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae is regulated by amino acid abundance. When amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesic...
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| Format: | Article |
| Language: | en_US |
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American Society for Cell Biology
2011
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| Online Access: | http://hdl.handle.net/1721.1/65651 https://orcid.org/0000-0002-1505-0479 |
| _version_ | 1826205247481053184 |
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| author | Cain, Natalie Elaine Kaiser, Chris |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Cain, Natalie Elaine Kaiser, Chris |
| author_sort | Cain, Natalie Elaine |
| collection | MIT |
| description | Intracellular trafficking of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae is regulated by amino acid abundance. When amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome (MVE) and to the vacuole. Here we test the hypothesis that Gap1p itself is the sensor of amino acid abundance by examining the trafficking of Gap1p mutants with altered substrate specificity and transport activity. We show that trafficking of mutant Gap1pA297V, which does not transport basic amino acids, is also not regulated by these amino acids. Furthermore, we have identified a catalytically inactive mutant that does not respond to complex amino acid mixtures and constitutively sorts Gap1p to the plasma membrane. Previously we showed that amino acids govern the propensity of Gap1p to recycle from the MVE to the plasma membrane. Here we propose that in the presence of substrate the steady-state conformation of Gap1p shifts to a state that is unable to be recycled from the MVE. These results indicate a parsimonious regulatory mechanism by which Gap1p senses its transport substrates to set an appropriate level of transporter activity at the cell surface. |
| first_indexed | 2024-09-23T13:10:00Z |
| format | Article |
| id | mit-1721.1/65651 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T13:10:00Z |
| publishDate | 2011 |
| publisher | American Society for Cell Biology |
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| spelling | mit-1721.1/656512022-09-28T12:20:52Z Transport activity-dependent intracellular sorting of the yeast general amino acid permease Cain, Natalie Elaine Kaiser, Chris Massachusetts Institute of Technology. Department of Biology Kaiser, Chris Kaiser, Chris Cain, Natalie Elaine Intracellular trafficking of the general amino acid permease, Gap1p, of Saccharomyces cerevisiae is regulated by amino acid abundance. When amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome (MVE) and to the vacuole. Here we test the hypothesis that Gap1p itself is the sensor of amino acid abundance by examining the trafficking of Gap1p mutants with altered substrate specificity and transport activity. We show that trafficking of mutant Gap1pA297V, which does not transport basic amino acids, is also not regulated by these amino acids. Furthermore, we have identified a catalytically inactive mutant that does not respond to complex amino acid mixtures and constitutively sorts Gap1p to the plasma membrane. Previously we showed that amino acids govern the propensity of Gap1p to recycle from the MVE to the plasma membrane. Here we propose that in the presence of substrate the steady-state conformation of Gap1p shifts to a state that is unable to be recycled from the MVE. These results indicate a parsimonious regulatory mechanism by which Gap1p senses its transport substrates to set an appropriate level of transporter activity at the cell surface. National Institutes of Health (U.S.) (grant GM56933) 2011-09-12T20:30:12Z 2011-09-12T20:30:12Z 2011-06 Article http://purl.org/eprint/type/JournalArticle 1059-1524 1939-4586 http://hdl.handle.net/1721.1/65651 Cain, N. E., and C. A. Kaiser. “Transport activity-dependent intracellular sorting of the yeast general amino acid permease.” Molecular Biology of the Cell 22 (2011): 1919-1929. https://orcid.org/0000-0002-1505-0479 en_US http://dx.doi.org/10.1091/mbc.E10-10-0800 Molecular Biology of the Cell Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Society for Cell Biology ASCB |
| spellingShingle | Cain, Natalie Elaine Kaiser, Chris Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title | Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title_full | Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title_fullStr | Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title_full_unstemmed | Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title_short | Transport activity-dependent intracellular sorting of the yeast general amino acid permease |
| title_sort | transport activity dependent intracellular sorting of the yeast general amino acid permease |
| url | http://hdl.handle.net/1721.1/65651 https://orcid.org/0000-0002-1505-0479 |
| work_keys_str_mv | AT cainnatalieelaine transportactivitydependentintracellularsortingoftheyeastgeneralaminoacidpermease AT kaiserchris transportactivitydependentintracellularsortingoftheyeastgeneralaminoacidpermease |