Characterization of the Novel Polyglutamine Protein FAM171B
Location
CSU Ballroom
Start Date
9-4-2012 10:00 AM
End Date
9-4-2012 11:30 AM
Student's Major
Biological Sciences
Student's College
Science, Engineering and Technology
Mentor's Name
Geoffrey Goellner
Mentor's Department
Biological Sciences
Mentor's College
Science, Engineering and Technology
Description
FAM171B is a completely uncharacterized protein (identified via the human genome sequencing project) that contains a polyglutamine (polyQ) stretch within its primary amino acid sequence. PolyQ tract proteins are particularly interesting, as expansion mutations within them have been shown to underlie a growing number of severe neurodegenerative disorders such as Huntingtons Disease and Spinocerebellar Ataxia. Using a bioinformatics approach, we find that FAM171B not only contains a polyQ region near its amino-terminus, but also is likely expressed in the nervous system and contains both a putative signal sequence and a single transmembrane domain. These data suggest that FAM171B normally functions within the endomembrane system of neurons- and mutations within the polyQ tract may underlie an as yet molecularly uncharacterized neurodegenerative disease. In this study, we set out to not only shed light on the normal cellular function of FAM171B (by identifying its intracellular localization), but also to assay the degree of polymorphism within its polyQ tract (an indication of expansion mutation propensity). Using immunofluorescence assays, we find that FAM171B displays a punctate vesicular-like staining pattern within the cytoplasm of HELA and HEK cells- consistent with bioinformatics predictions. In addition, using DNA genotyping assays, we find that the polyQ tract within FAM171B is quite stable within the human population (96.5% homogeneity)- suggesting FAM171B should not be considered a strong candidate gene for neurodegenerative disease. The preliminary outcomes, from the combined studies of localization and polymorphism, characterize FAM171B as a stable cytoplasmic protein localizing to vesicular organelles- such as, mitochondria or endosomes.
Characterization of the Novel Polyglutamine Protein FAM171B
CSU Ballroom
FAM171B is a completely uncharacterized protein (identified via the human genome sequencing project) that contains a polyglutamine (polyQ) stretch within its primary amino acid sequence. PolyQ tract proteins are particularly interesting, as expansion mutations within them have been shown to underlie a growing number of severe neurodegenerative disorders such as Huntingtons Disease and Spinocerebellar Ataxia. Using a bioinformatics approach, we find that FAM171B not only contains a polyQ region near its amino-terminus, but also is likely expressed in the nervous system and contains both a putative signal sequence and a single transmembrane domain. These data suggest that FAM171B normally functions within the endomembrane system of neurons- and mutations within the polyQ tract may underlie an as yet molecularly uncharacterized neurodegenerative disease. In this study, we set out to not only shed light on the normal cellular function of FAM171B (by identifying its intracellular localization), but also to assay the degree of polymorphism within its polyQ tract (an indication of expansion mutation propensity). Using immunofluorescence assays, we find that FAM171B displays a punctate vesicular-like staining pattern within the cytoplasm of HELA and HEK cells- consistent with bioinformatics predictions. In addition, using DNA genotyping assays, we find that the polyQ tract within FAM171B is quite stable within the human population (96.5% homogeneity)- suggesting FAM171B should not be considered a strong candidate gene for neurodegenerative disease. The preliminary outcomes, from the combined studies of localization and polymorphism, characterize FAM171B as a stable cytoplasmic protein localizing to vesicular organelles- such as, mitochondria or endosomes.
Recommended Citation
Lee, Han Byul. "Characterization of the Novel Polyglutamine Protein FAM171B." Undergraduate Research Symposium, Mankato, MN, April 9, 2012.
https://cornerstone.lib.mnsu.edu/urs/2012/poster-session-A/12
