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Studies on proteins transporting carnitine to the cell, in particular on organic cation/carnitine transporter – OCTN2 (SLC22A5) and amino acid transporter B(0,+) – ATB(0,+) (SLC6A14). The experiments have been focused on the mechanism of transporters trafficking to plasma membrane and the role of other proteins in this process. The main goal is to establish the role of transporters domains in interaction with other protein. The role of OCTN2 and ATB(0,+) in cancer cells is also investigated.
- cell culture (primary culture of brain cells and cells transfected with vectors containing the studied genes)
- preparing vectors with mutated genes coding studied transporters
- transport measurements
- quantitative estimation of gene expression
- proteomics of hydrophobic proteins
- studies on the mechanism of ATB(0,+) exit from endoplasmic reticulum
- studies on interaction of OCTN2 with PDZ-domain containing proteins
- studies on OCTN2 proteome and transporter interaction with PP2A phosphatase
- studies on ATB(0,+) in cancer cells
Juraszek B., Czarnecka-Herok J. Nałęcz K.A. (2021) Glioma cells survival depends both on fatty acid oxidation and on functional carnitine transport by SLC22A5, J. Neurochem. 156, 642-657, doi: 10.1111/jnc.15124.
Juraszek B., Nałęcz K.A. (2020) SLC22A5 (OCTN2) Carnitine Transporter – indispensable for cell metabolism, a Jekyll and Hyde of human cancer, Molecules, 2020, 25,14; doi:10.3390/molecules25010014.
Nałęcz K.A. (2020) Amino acid transporter SLCA14 (ATB0,+) – A target in combined anti-cancer therapy, Front. Cell Dev. Biol.; 8:594464, doi: 10.3389/fcell.2020.594464.
Kovalchuk V., Samluk Ł., Juraszek B., Jurkiewicz-Trząska D., Sucic S., Freissmuth M. Nałęcz K.A. (2019), Trafficking of the amino acid transporter B(0,+) (SLC6A14) to the plasma membrane involves an exclusive interaction with SEC24C for its exit from the endoplasmic reticulum BBA – Mol. Cell Res., 1866, 252-263, doi: 10.1016/j.bbamcr.2018.11.005.
Rogala-Koziarska K. Samluk Ł. Nałęcz K.A. (2019) Amino acid transporter SLC6A14 depends on heat shock protein HSP90 in trafficking to the cell surface, BBA – Mol. Cell Res., 1866, 1544-1555, doi: 10.1016/j.bbamcr.201908.009.