| Work reveals that cross-linking of microtubules by MAP65-1 confers resistance to severing by inhibiting the binding of KTN1 and identifies the structural features of MAP65-1 that are important for this activity. | Microtubule bundling by MAP65-1 protects against severing by inhibiting the binding of katanin.
Burkart GM, Dixit R., Free PMC Article | 01/11/2020 |
| MAP65-1 plays a critical role in the response to salt stress and is required for regulating the rapid depolymerization and reorganization of cortical microtubules (MTs). | MAP65-1 is required for the depolymerization and reorganization of cortical microtubules in the response to salt stress in Arabidopsis.
Zhou S, Chen Q, Li X, Li Y. | 03/31/2018 |
| MAP65-1 is subject to multiple phosphorylation events by Aurora kinases during consecutive stages of the cell cycle. | Phosphorylation of MAP65-1 by Arabidopsis Aurora Kinases Is Required for Efficient Cell Cycle Progression.
Boruc J, Weimer AK, Stoppin-Mellet V, Mylle E, Kosetsu K, Cedeño C, Jaquinod M, Njo M, De Milde L, Tompa P, Gonzalez N, Inzé D, Beeckman T, Vantard M, Van Damme D., Free PMC Article | 12/2/2017 |
| Data indicate that microtubules (MTs) bundle flexibility is differently regulated, depending on MAP65 cross-linker. | MAP65/Ase1 promote microtubule flexibility.
Portran D, Zoccoler M, Gaillard J, Stoppin-Mellet V, Neumann E, Arnal I, Martiel JL, Vantard M., Free PMC Article | 01/18/2014 |
| PLDalpha1-derived phosphatidic acid (PA) binds to MAP65-1, thus mediating microtubule stabilization and salt tolerance. It reveals a functional connection between membrane lipids and the cytoskeleton in environmental stress signaling. | Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis.
Zhang Q, Lin F, Mao T, Nie J, Yan M, Yuan M, Zhang W., Free PMC Article | 08/31/2013 |
| MAP65-1 and MAP65-2 play a critical role in the microtubule-dependent mechanism for specifying axial cell growth in the expanding hypocotyl, independent of any mechanical role in microtubule array organization. | Microtubule-associated proteins MAP65-1 and MAP65-2 positively regulate axial cell growth in etiolated Arabidopsis hypocotyls.
Lucas JR, Courtney S, Hassfurder M, Dhingra S, Bryant A, Shaw SL., Free PMC Article | 01/12/2013 |
| MAP65-1 and MAP65-2 play a critical role in root growth by promoting cell proliferation and axial extension. | MAP65-1 and MAP65-2 promote cell proliferation and axial growth in Arabidopsis roots.
Lucas JR, Shaw SL. | 12/22/2012 |
| Results also show that MAP65-1 and MAP65-3 may share redundant functions in MT stabilization. | Arabidopsis microtubule-associated protein MAP65-3 cross-links antiparallel microtubules toward their plus ends in the phragmoplast via its distinct C-terminal microtubule binding domain.
Ho CM, Lee YR, Kiyama LD, Dinesh-Kumar SP, Liu B., Free PMC Article | 10/27/2012 |
| the rod domain of MAP65-1 acts both as a spacer and as a structural element that specifies the microtubule encounter angles that are conducive for bundling | Single-molecule analysis of the microtubule cross-linking protein MAP65-1 reveals a molecular mechanism for contact-angle-dependent microtubule bundling.
Tulin A, McClerklin S, Huang Y, Dixit R., Free PMC Article | 06/9/2012 |
| MAP65-1 binds cortical microtubules. | [Localization of microtubule-associated protein AtMAP65-1 in guard cells of arabidopsis].
Yu R, Sun L, Li XD, Wang XC, Yuan M, Wu ZY. | 01/21/2010 |
| AtMAP65-1 and AtMAP65-5 promote antiparallel microtubule bundling | Two microtubule-associated proteins of Arabidopsis MAP65s promote antiparallel microtubule bundling.
Gaillard J, Neumann E, Van Damme D, Stoppin-Mellet V, Ebel C, Barbier E, Geelen D, Vantard M., Free PMC Article | 01/21/2010 |
| The predicted three-dimensional structure of AtMAP65-1 was used as a basis for analyzing the actual cross-bridging with microtubules in detail. | The AtMAP65-1 cross-bridge between microtubules is formed by one dimer.
Li H, Mao T, Zhang Z, Yuan M. | 01/21/2010 |
| AtMAP65-1 plays a role in the central spindle at anaphase to early cytokinesis but is not essential at the midline of the phragmoplast at later stages. | Modulated targeting of GFP-AtMAP65-1 to central spindle microtubules during division.
Mao G, Chan J, Calder G, Doonan JH, Lloyd CW. | 01/21/2010 |
| Data suggest that normal metaphase spindle organisation and the transition to anaphase is dependent on inactivation of AtMAP65-1 | Control of the AtMAP65-1 interaction with microtubules through the cell cycle.
Smertenko AP, Chang HY, Sonobe S, Fenyk SI, Weingartner M, Bögre L, Hussey PJ. | 01/21/2010 |
| evidence that AtMAP65-1 and AtMAP65-6, two related proteins, may regulate microtubule organization in different manners | Two microtubule-associated proteins of the Arabidopsis MAP65 family function differently on microtubules.
Mao T, Jin L, Li H, Liu B, Yuan M., Free PMC Article | 01/21/2010 |
| AtMAP65-1 might promote tubulin assembly by binding to tubulin dimers in vivo.[AtMAP65-1] | AtMAP65-1 binds to tubulin dimers to promote tubulin assembly.
Li H, Yuan M, Mao T. | 01/21/2010 |