Event Title

Structural Insights Into the Functions of Microtubule and Microtubule-Associated Proteins

Session Number

B01

Advisor(s)

Ao Ma, University of Illinois at Chicago
Ken Tsui, University of Illinois at Chicago
Xinge Wang, University of Illinois at Chicago

Location

B-101

Start Date

28-4-2016 9:50 AM

End Date

28-4-2016 10:15 AM

Disciplines

Biomedical Engineering and Bioengineering

Abstract

Microtubules (MTs) are polymers of tubulin that exhibit highly dynamic instability and play a critical role in the eukaryotic cell cycle. MT dynamic instability, which is the fluctuation between growth and shrinkage of MT ends, allows cells to undergo constant, rapid structural reorganization to perform various cell functions. MT plus-end tracking proteins (+TIPs) are a type of microtubule- associated protein (MAP) that modulates MT dynamics and link cellular components to the MT tip. Members of one class of +TIPs are known as the end-binding (EB) proteins, which play a significant role in the protein-protein interaction dynamic network. In order to understand how EB tubulin complex affects MT function, we’ve pieced together information from various scholarly articles. Furthermore, by using the digital visualization software, Chimera, to visualize these structures, we have been better able to understand how the structure of tubulin changes. Our investigation into MT promotes more understanding about the relationship between subunit structure to MT dynamic instability. As a result, we have learned how different conformations of tubulin dimers change at MT plus end, how EBs bind to specific conformation of tubulins and specific part of MT only and how these bindings might affect tubulin conformation changes during MT growth phase and affect dynamic instability


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Apr 28th, 9:50 AM Apr 28th, 10:15 AM

Structural Insights Into the Functions of Microtubule and Microtubule-Associated Proteins

B-101

Microtubules (MTs) are polymers of tubulin that exhibit highly dynamic instability and play a critical role in the eukaryotic cell cycle. MT dynamic instability, which is the fluctuation between growth and shrinkage of MT ends, allows cells to undergo constant, rapid structural reorganization to perform various cell functions. MT plus-end tracking proteins (+TIPs) are a type of microtubule- associated protein (MAP) that modulates MT dynamics and link cellular components to the MT tip. Members of one class of +TIPs are known as the end-binding (EB) proteins, which play a significant role in the protein-protein interaction dynamic network. In order to understand how EB tubulin complex affects MT function, we’ve pieced together information from various scholarly articles. Furthermore, by using the digital visualization software, Chimera, to visualize these structures, we have been better able to understand how the structure of tubulin changes. Our investigation into MT promotes more understanding about the relationship between subunit structure to MT dynamic instability. As a result, we have learned how different conformations of tubulin dimers change at MT plus end, how EBs bind to specific conformation of tubulins and specific part of MT only and how these bindings might affect tubulin conformation changes during MT growth phase and affect dynamic instability