Inactivation of Tor Proteins Affects the Dynamics of Endocytic Proteins in Early Stage of Endocytosis

<p>Tor2 is an activator of the Rom2/Rho1 pathway that regulates α-factor internalization. Since the recruitment of endocytic proteins such as actin binding proteins and the amphiphysins precedes the internalization of α-factor, I hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. I report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants. Furthermore, I found that the endocytic proteins Rvs167 and Sjl2 are completely mistargeted to the cytoplasm in tor1∆tor2ts double mutant cells. I also demonstrate here that the efficiency of endocytic internalization or scission in all tor mutants was drastically decreased. In agreement with the Sjl2 mislocalization, I found that in tor1∆tor2ts double mutant cells, as well as other tor mutant cells, the overall PIP2 level was dramatically increased. Finally, the cell wall chitin content in tor2ts and tor1∆tor2ts mutant cells was also significantly increased. Taken together, both functional Tor proteins, Tor1 and Tor2, are essentially required for proper endocytic protein dynamics at the early stage of endocytosis.</p>

Name thesis:degree_name

Master of Science in Biology

Level thesis:degree_level

Masters

Discipline thesis:degree_discipline

Biology

Year

2013

Author dc:creator

• Tenay, Brandon Scott

Contributors dc:contributor

• Kyoungtae Kim

• Tor2
• endocytosis
• scission
• PIP2
• Abp1
• Biology

Statement dc:rights

• © Brandon Scott Tenay

Repository record dc:identifier

https://bearworks.missouristate.edu/theses/1312

OAI identifier oai:identifier

oai:bearworks.missouristate.edu:theses-2313