Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization
N-MYC DOWNREGULATED-LIKE proteins (NDL), members of the alpha/beta hydrolase superfamily were recently rediscovered as interactors of G-protein signaling in Arabidopsis thaliana. Although the precise molecular function of NDL proteins is still elusive, in animals these proteins play protective role...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-10-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00947/full |
| _version_ | 1818499692927909888 |
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| author | Nisha eKhatri Yashwanti eMudgil |
| author_facet | Nisha eKhatri Yashwanti eMudgil |
| author_sort | Nisha eKhatri |
| collection | DOAJ |
| description | N-MYC DOWNREGULATED-LIKE proteins (NDL), members of the alpha/beta hydrolase superfamily were recently rediscovered as interactors of G-protein signaling in Arabidopsis thaliana. Although the precise molecular function of NDL proteins is still elusive, in animals these proteins play protective role in hypoxia and expression is induced by hypoxia and nickel, indicating role in stress. Homology of NDL1 with animal counterpart NDRG suggests similar functions in animals and plants. It is well established that stress responses leads to the microtubule depolymerization and reorganization which is crucial for stress tolerance. NDRG is a microtubule-associated protein (MAP) which mediates the microtubule organization in animals by causing acetylation and increases the stability of α-tubulin. As NDL1 is highly homologous to NDRG, involvement of NDL1 in the microtubule organization during plant stress can also be expected. Discovery of interaction of NDL with protein kinesin light chain- related 1, enodomembrane family protein 70, syntaxin-23, tubulin alpha-2 chain, as a part of G protein interactome initiative encourages us to postulate microtubule stabilizing functions for NDL family in plants. Our search for NDL interactors in G protein interactome also predicts the role of NDL proteins in abiotic stress tolerance management. Based on published report in animals and predicted interacting partners for NDL in G protein interactome lead us to hypothesize involvement of NDL in the microtubule organization during abiotic stress management in plants. |
| first_indexed | 2024-12-10T20:32:54Z |
| format | Article |
| id | doaj.art-d7e8137ed99645718af39f06f34be463 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-10T20:32:54Z |
| publishDate | 2015-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-d7e8137ed99645718af39f06f34be4632022-12-22T01:34:38ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2015-10-01610.3389/fpls.2015.00947165472Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule OrganizationNisha eKhatri0Yashwanti eMudgil1Delhi UniversityDelhi UniversityN-MYC DOWNREGULATED-LIKE proteins (NDL), members of the alpha/beta hydrolase superfamily were recently rediscovered as interactors of G-protein signaling in Arabidopsis thaliana. Although the precise molecular function of NDL proteins is still elusive, in animals these proteins play protective role in hypoxia and expression is induced by hypoxia and nickel, indicating role in stress. Homology of NDL1 with animal counterpart NDRG suggests similar functions in animals and plants. It is well established that stress responses leads to the microtubule depolymerization and reorganization which is crucial for stress tolerance. NDRG is a microtubule-associated protein (MAP) which mediates the microtubule organization in animals by causing acetylation and increases the stability of α-tubulin. As NDL1 is highly homologous to NDRG, involvement of NDL1 in the microtubule organization during plant stress can also be expected. Discovery of interaction of NDL with protein kinesin light chain- related 1, enodomembrane family protein 70, syntaxin-23, tubulin alpha-2 chain, as a part of G protein interactome initiative encourages us to postulate microtubule stabilizing functions for NDL family in plants. Our search for NDL interactors in G protein interactome also predicts the role of NDL proteins in abiotic stress tolerance management. Based on published report in animals and predicted interacting partners for NDL in G protein interactome lead us to hypothesize involvement of NDL in the microtubule organization during abiotic stress management in plants.http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00947/fullabiotic stressmicrotubule assemblyPhospholipase D (PLD)Microtubule-associated protein (MAP)Phosphatidic acid (PA)N-MYC DOWNREGULATED GENE (NDRG) |
| spellingShingle | Nisha eKhatri Yashwanti eMudgil Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization Frontiers in Plant Science abiotic stress microtubule assembly Phospholipase D (PLD) Microtubule-associated protein (MAP) Phosphatidic acid (PA) N-MYC DOWNREGULATED GENE (NDRG) |
| title | Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization |
| title_full | Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization |
| title_fullStr | Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization |
| title_full_unstemmed | Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization |
| title_short | Hypothesis: NDL Proteins Function in Stress Responses by Regulating Microtubule Organization |
| title_sort | hypothesis ndl proteins function in stress responses by regulating microtubule organization |
| topic | abiotic stress microtubule assembly Phospholipase D (PLD) Microtubule-associated protein (MAP) Phosphatidic acid (PA) N-MYC DOWNREGULATED GENE (NDRG) |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00947/full |
| work_keys_str_mv | AT nishaekhatri hypothesisndlproteinsfunctioninstressresponsesbyregulatingmicrotubuleorganization AT yashwantiemudgil hypothesisndlproteinsfunctioninstressresponsesbyregulatingmicrotubuleorganization |