Maxim Sokolov, PhD
PO Box 9193
WVU Eye Institute
Morgantown, WV 26506
- Molecular Chaperones
- Heterotrimeric G Proteins
- Retinal Photoreceptors
1. Developing therapies utilizing microbial molecular chaperones
Molecular chaperones allow unicellular organisms (microbes) to survive environmental insults that perturb proteostasis, however, some types of microbial chaperones are not found in mammalian genomes. We are interested in exploring the therapeutic potential of xenogeneic chaperones against neurodegenerative diseases caused by protein misfolding and deregulation of proteostasis. The goal of this project is to evaluate the efficiency of a chaperon from thermophilic archaea to counteract the progression of neurodegenerative congenital blinding disease in mouse models.
2. Chaperonin system of rod photoreceptors
Eukaryotic chaperonin containing t-complex protein 1 (CCT/TRiC) is a ring-shaped ATPase complex, which folds nascent polypeptides, while they are encapsulated in the central cavity. CCT is known to fold a range of proteins including actin, tubulin, and heterotrimeric G proteins. Nevertheless, many CCT substrates and regulatory co-factors in specialized mammalian cells remain unknown. This project focuses on the molecular and cellular mechanisms that regulate the substrate specificity of CCT. It exploits a transgenic mouse model which allows us to study protein interactions of CCT by mass spectrometry.
- Brooks, C., Snoberger, A., Belcastro, M., Murphy, J., Kisselev, O., Smith, D., Sokolov, M. (2018) “Archaeal Unfoldase Counteracts Protein Misfolding Retinopathy in Mice.” Journal of Neuroscience 38(33) 7248-7254, (PMID: 30012684)
- Brooks, C., Murphy, J., Belcastro, M., Heller, D., Kolandaivelu, S., Kisselev, O., Sokolov, M. (2018) “Farnesylation of the Transducin G Protein Gamma Subunit Is a Prerequisite for Its Ciliary Targeting in Rod Photoreceptors.” Frontiers in Molecular Neuroscience 11 (16) PMCID: PMC5787109
- Wright ZC, SIngh RK, Alpino R, Goldberg AF, Sokolov M, Ramamurthy V. ARL3 regulates trafficking of prenylated phototransduction proteins to the rod outer segment. Hum Mol Genet (2016) [Epub ahead of print].
- Sinha S, Belcastro M, Datta P, Seo S, Sokolov M. Essential role of the chaperonin CCT in rod outer segment biogenesis. Invest Ophthalmol Vis Sci (2014) 55(6): 3775-85. PMCID: PMC4062400.
- Gao X, Sinha S, Belcastro M, Woodard C, Ramamurthy V, Stoilov P, Sokolov M. Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins. J Biol Chem (2013 Sep 6); 288(36):25760-8.
- Sinha S, Majumder A, Belcastro M, Sokolov M, Artemyev NO. Expression and subcellular distribution of UNC119a, a protein partner of transducin α subunit in rod photoreceptors. Cell Signal (2013 Jan) 25(1): 341-8. doi: 10.1016/j.cellsig.2012.10.005.
- Belcastro M, Song H, Sinha S, Song C, Mathers PH, Sokolov M. Phosphorylation of phosducin accelerates rod recovery from transducin translocation. Invest Ophthalmol Vis Sci (2012 May 1) 53(6): 3084-91. doi: 10.1167/iovs.11-8798.
- Yang J, Wang L, Song H, Sokolov M. Current understanding of usher syndrome type II. Front Biosci (2012 Jan 1) 17:1165-83.
- Posokhova E, Song H, Belcastro M, Higgins L, Bigley LR, Michaud NA, Martemyanov KA, Sokolov M. Disruption of the chaperonin containing TCP-1 function affects protein networks essential for Rod outer segment morphogenesis and survival. Mol Cell Proteomics. 2010 Sep 17.
- Edrington TC, Sokolov M, Boesze-Battaglia K. Peripherin/rds co-distributes with putative binding partners in basal rod outer segment disks. Exp Eye Res (2011) 92(5):439-42.