MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network
Selective autophagy is a process whereby specific targeted cargo proteins, aggregates, or organelles are sequestered into double-membrane-bound phagophores before fusion with the lysosome for protein degradation. It has been demonstrated that the microtubule network is important for the formation an...
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| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | International Journal of Cell Biology |
| Online Access: | http://dx.doi.org/10.1155/2012/208014 |
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| _version_ | 1832562768224452608 |
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| author | Katie Marchbank Sarah Waters Roland G. Roberts Ellen Solomon Caroline A. Whitehouse |
| author_facet | Katie Marchbank Sarah Waters Roland G. Roberts Ellen Solomon Caroline A. Whitehouse |
| author_sort | Katie Marchbank |
| collection | DOAJ |
| description | Selective autophagy is a process whereby specific targeted cargo proteins, aggregates, or organelles are sequestered into double-membrane-bound phagophores before fusion with the lysosome for protein degradation. It has been demonstrated that the microtubule network is important for the formation and movement of autophagosomes. Nbr1 is a selective cargo receptor that through its interaction with LC3 recruits ubiquitinated proteins for autophagic degradation. This study demonstrates an interaction between the evolutionarily conserved FW domain of Nbr1 with the microtubule-associated protein MAP1B. Upon autophagy induction, MAP1B localisation is focused into discrete vesicles with Nbr1. This colocalisation is dependent upon an intact microtubule network as depolymerisation by nocodazole treatment abolishes starvation-induced MAP1B recruitment to these vesicles. MAP1B is not recruited to autophagosomes for protein degradation as blockage of lysosomal acidification does not result in significant increased MAP1B protein levels. However, the protein levels of phosphorylated MAP1B are significantly increased upon blockage of autophagic degradation. This is the first evidence that links the ubiquitin receptor Nbr1, which shuttles ubiquitinated proteins to be degraded by autophagy, to the microtubule network. |
| format | Article |
| id | doaj-art-ca57f79e25b6416aaf7ace98451a6c9e |
| institution | Kabale University |
| issn | 1687-8876 1687-8884 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Cell Biology |
| spelling | doaj-art-ca57f79e25b6416aaf7ace98451a6c9e2025-02-03T01:21:54ZengWileyInternational Journal of Cell Biology1687-88761687-88842012-01-01201210.1155/2012/208014208014MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule NetworkKatie Marchbank0Sarah Waters1Roland G. Roberts2Ellen Solomon3Caroline A. Whitehouse4Department of Medical and Molecular Genetics, Kings College London, London SE1 9RT, UKThe Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, British Heart Foundation Centre of Research Excellence, King’s College London, London SE1 1UL, UKDepartment of Medical and Molecular Genetics, Kings College London, London SE1 9RT, UKDepartment of Medical and Molecular Genetics, Kings College London, London SE1 9RT, UKDepartment of Medical and Molecular Genetics, Kings College London, London SE1 9RT, UKSelective autophagy is a process whereby specific targeted cargo proteins, aggregates, or organelles are sequestered into double-membrane-bound phagophores before fusion with the lysosome for protein degradation. It has been demonstrated that the microtubule network is important for the formation and movement of autophagosomes. Nbr1 is a selective cargo receptor that through its interaction with LC3 recruits ubiquitinated proteins for autophagic degradation. This study demonstrates an interaction between the evolutionarily conserved FW domain of Nbr1 with the microtubule-associated protein MAP1B. Upon autophagy induction, MAP1B localisation is focused into discrete vesicles with Nbr1. This colocalisation is dependent upon an intact microtubule network as depolymerisation by nocodazole treatment abolishes starvation-induced MAP1B recruitment to these vesicles. MAP1B is not recruited to autophagosomes for protein degradation as blockage of lysosomal acidification does not result in significant increased MAP1B protein levels. However, the protein levels of phosphorylated MAP1B are significantly increased upon blockage of autophagic degradation. This is the first evidence that links the ubiquitin receptor Nbr1, which shuttles ubiquitinated proteins to be degraded by autophagy, to the microtubule network.http://dx.doi.org/10.1155/2012/208014 |
| spellingShingle | Katie Marchbank Sarah Waters Roland G. Roberts Ellen Solomon Caroline A. Whitehouse MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network International Journal of Cell Biology |
| title | MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network |
| title_full | MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network |
| title_fullStr | MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network |
| title_full_unstemmed | MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network |
| title_short | MAP1B Interaction with the FW Domain of the Autophagic Receptor Nbr1 Facilitates Its Association to the Microtubule Network |
| title_sort | map1b interaction with the fw domain of the autophagic receptor nbr1 facilitates its association to the microtubule network |
| url | http://dx.doi.org/10.1155/2012/208014 |
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