Jump to content
Main menu
Main menu
move to sidebar
hide
Navigation
Main page
Recent changes
Random page
Help about MediaWiki
Special pages
Niidae Wiki
Search
Search
Appearance
Create account
Log in
Personal tools
Create account
Log in
Pages for logged out editors
learn more
Contributions
Talk
Editing
Microtubule
(section)
Page
Discussion
English
Read
Edit
View history
Tools
Tools
move to sidebar
hide
Actions
Read
Edit
View history
General
What links here
Related changes
Page information
Appearance
move to sidebar
hide
Warning:
You are not logged in. Your IP address will be publicly visible if you make any edits. If you
log in
or
create an account
, your edits will be attributed to your username, along with other benefits.
Anti-spam check. Do
not
fill this in!
===Dynamic instability=== [[File:MicrotubuleDynamicInstability.ogv|thumb|Animation of the microtubule dynamic instability. Tubulin dimers bound to GTP (red) bind to the growing end of a microtubule and subsequently hydrolyze GTP into GDP (blue).]] Dynamic instability refers to the coexistence of assembly and disassembly at the ends of a microtubule. The microtubule can dynamically switch between growing and shrinking phases in this region.<ref>{{Cite book |url=https://archive.org/details/cellmolecularbio04edkarp/page/355 |title=Cell and Molecular Biology: Concepts and Experiments |vauthors=Karp G |publisher=John Wiley & Sons |year=2005 |isbn=978-0-471-46580-5 |location=USA |page=[https://archive.org/details/cellmolecularbio04edkarp/page/355 355]}}</ref> Tubulin dimers can bind two molecules of GTP, one of which can be hydrolyzed subsequent to assembly. During polymerization, the tubulin dimers are in the [[Guanosine triphosphate|GTP]]-bound state.<ref name="weisenberg" /> The GTP bound to Ξ±-tubulin is stable and it plays a structural function in this bound state. However, the GTP bound to Ξ²-tubulin may be [[hydrolysis|hydrolyzed]] to [[Guanosine diphosphate|GDP]] shortly after assembly. The assembly properties of GDP-tubulin are different from those of GTP-tubulin, as GDP-tubulin is more prone to depolymerization.<ref>{{Cite journal |vauthors=Weisenberg RC, Deery WJ, Dickinson PJ |date=September 1976 |title=Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubules |journal=Biochemistry |volume=15 |issue=19 |pages=4248β54 |doi=10.1021/bi00664a018 |pmid=963034}}</ref> A GDP-bound tubulin subunit at the tip of a microtubule will tend to fall off, although a GDP-bound tubulin in the middle of a microtubule cannot spontaneously pop out of the polymer. Since tubulin adds onto the end of the microtubule in the GTP-bound state, a cap of GTP-bound tubulin is proposed to exist at the tip of the microtubule, protecting it from disassembly. When hydrolysis catches up to the tip of the microtubule, it begins a rapid depolymerization and shrinkage. This switch from growth to shrinking is called a catastrophe. GTP-bound tubulin can begin adding to the tip of the microtubule again, providing a new cap and protecting the microtubule from shrinking. This is referred to as "rescue".<ref name="pmid6504138">{{Cite journal |vauthors=Mitchison T, Kirschner M |year=1984 |title=Dynamic instability of microtubule growth |journal=Nature |volume=312 |issue=5991 |pages=237β42 |bibcode=1984Natur.312..237M |doi=10.1038/312237a0 |pmid=6504138 |s2cid=30079133}}</ref>
Summary:
Please note that all contributions to Niidae Wiki may be edited, altered, or removed by other contributors. If you do not want your writing to be edited mercilessly, then do not submit it here.
You are also promising us that you wrote this yourself, or copied it from a public domain or similar free resource (see
Encyclopedia:Copyrights
for details).
Do not submit copyrighted work without permission!
Cancel
Editing help
(opens in new window)
Search
Search
Editing
Microtubule
(section)
Add topic