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Localization of different conformation forms of Transglutaminase 2 in living cells
Author(s) -
Pavlyukov Marat S,
Shakhparonov Mihail I,
Shemyakin M.M.,
Yu A
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.798.2
Subject(s) - tissue transglutaminase , cytoplasm , subcellular localization , endosome , enzyme , microbiology and biotechnology , apoptosis , biochemistry , lysine , cell , chemistry , biology , amino acid
Transglutaminase (TG2) is a ubiquitously expressed enzyme that has been implicated in a variety of biological disorders ranging from inflammatory and cancer to neurodegenerative diseases. Initially TG2 was described as a Ca 2+ ‐dependent transamidating enzyme (EC 2.3.2.13) that catalyzes protein cross‐linking via formation of an isopeptide bond between a specific glutamyl containing peptide substrate and a ε‐amine group of a protein‐bound lysine residue. Later investigations have showed that TG2 possesses other biochemical functions and participates in several cell processes. However, it is steel a matter of discussion what process requires TG2 crosslinking activity. But it is now clear that activated and inactivated TG2 are present in different conformational states. We have developed a new FRET based method for observing the changes in TG2 conformation in living cells. Using that method we studied localization of different conformation forms of TG2 in cells in «healthy» conditions and after apoptosis induction. We have shown that there are distinct subcellular pools of TG2 that localize in the cytoplasm, perinuclear endosomes and under the cellular membrane. After apoptosis induction rapid activation of cytoplasmic TG2 occurs. Ongoing work further investigates the exact role of different TG2 pools in apoptosis regulation. [Supported by Russian Foundation for Basic Research grant 10‐04‐01206]