Nucleation and dynamics of Golgi-derived microtubules
Integrity of the Golgi apparatus requires the microtubule (MT) network. A subset of MTs originates at the Golgi itself, which in this case functions as a MT-organizing center (MTOC). Golgi-derived MTs serve important roles in post-Golgi trafficking, maintenance of Golgi integrity, cell polarity and...
| Published in: | Frontiers in Neuroscience |
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| Main Authors: | , |
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2015-11-01
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| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00431/full |
| _version_ | 1857011853860798464 |
|---|---|
| author | Anna A.W.M. Sanders Irina eKaverina |
| author_facet | Anna A.W.M. Sanders Irina eKaverina |
| author_sort | Anna A.W.M. Sanders |
| collection | DOAJ |
| container_title | Frontiers in Neuroscience |
| description | Integrity of the Golgi apparatus requires the microtubule (MT) network. A subset of MTs originates at the Golgi itself, which in this case functions as a MT-organizing center (MTOC). Golgi-derived MTs serve important roles in post-Golgi trafficking, maintenance of Golgi integrity, cell polarity and motility, as well as cell type-specific functions, including neurite outgrowth/branching. Here, we discuss possible models describing the formation and dynamics of Golgi-derived MTs. How Golgi-derived MTs are formed is not fully understood. A widely discussed model implicates that the critical step of the process is recruitment of mo-lecular factors, which drive MT nucleation (γ-tubulin ring complex, or γ-TuRC), to the Golgi membrane via specific scaffolding interactions. Based on recent findings, we propose to introduce an additional level of regulation, whereby MT-binding proteins and/or local tubulin dimer concentration at the Golgi helps to overcome kinetic barriers at the initial nucleation step. According to our model, emerging MTs are subsequently stabilized by Golgi-associated MT-stabilizing proteins. We discuss molecular factors potentially involved in all three steps of MT formation. To preserve proper cell functioning, a balance must be maintained between MT subsets at the centrosome and the Golgi. Recent work has shown that certain centrosomal factors are important in maintaining this balance, suggesting a close connection between regulation of centrosomal and Golgi-derived MTs. Finally, we will discuss potential functions of Golgi-derived MTs based on their nucleation site location within a Golgi stack. |
| format | Article |
| id | doaj-art-9e4d4d96ffbd45fda8152f4cb1bedf21 |
| institution | Directory of Open Access Journals |
| issn | 1662-453X |
| language | English |
| publishDate | 2015-11-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| spelling | doaj-art-9e4d4d96ffbd45fda8152f4cb1bedf212025-08-19T19:46:41ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2015-11-01910.3389/fnins.2015.00431166177Nucleation and dynamics of Golgi-derived microtubulesAnna A.W.M. Sanders0Irina eKaverina1Vanderbilt University Medical CenterVanderbilt University Medical CenterIntegrity of the Golgi apparatus requires the microtubule (MT) network. A subset of MTs originates at the Golgi itself, which in this case functions as a MT-organizing center (MTOC). Golgi-derived MTs serve important roles in post-Golgi trafficking, maintenance of Golgi integrity, cell polarity and motility, as well as cell type-specific functions, including neurite outgrowth/branching. Here, we discuss possible models describing the formation and dynamics of Golgi-derived MTs. How Golgi-derived MTs are formed is not fully understood. A widely discussed model implicates that the critical step of the process is recruitment of mo-lecular factors, which drive MT nucleation (γ-tubulin ring complex, or γ-TuRC), to the Golgi membrane via specific scaffolding interactions. Based on recent findings, we propose to introduce an additional level of regulation, whereby MT-binding proteins and/or local tubulin dimer concentration at the Golgi helps to overcome kinetic barriers at the initial nucleation step. According to our model, emerging MTs are subsequently stabilized by Golgi-associated MT-stabilizing proteins. We discuss molecular factors potentially involved in all three steps of MT formation. To preserve proper cell functioning, a balance must be maintained between MT subsets at the centrosome and the Golgi. Recent work has shown that certain centrosomal factors are important in maintaining this balance, suggesting a close connection between regulation of centrosomal and Golgi-derived MTs. Finally, we will discuss potential functions of Golgi-derived MTs based on their nucleation site location within a Golgi stack.http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00431/fullGolgi ApparatusMicrotubulesmicrotubule dynamicsCLASP1ClaspsCLASP2 |
| spellingShingle | Anna A.W.M. Sanders Irina eKaverina Nucleation and dynamics of Golgi-derived microtubules Golgi Apparatus Microtubules microtubule dynamics CLASP1 Clasps CLASP2 |
| title | Nucleation and dynamics of Golgi-derived microtubules |
| title_full | Nucleation and dynamics of Golgi-derived microtubules |
| title_fullStr | Nucleation and dynamics of Golgi-derived microtubules |
| title_full_unstemmed | Nucleation and dynamics of Golgi-derived microtubules |
| title_short | Nucleation and dynamics of Golgi-derived microtubules |
| title_sort | nucleation and dynamics of golgi derived microtubules |
| topic | Golgi Apparatus Microtubules microtubule dynamics CLASP1 Clasps CLASP2 |
| url | http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00431/full |
| work_keys_str_mv | AT annaawmsanders nucleationanddynamicsofgolgiderivedmicrotubules AT irinaekaverina nucleationanddynamicsofgolgiderivedmicrotubules |
