FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor. 2009

Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany.

FKBP36 has been previously shown to be a crucial factor in spermatogenesis because of its interplay with the synaptonemal complex protein SCPI. Here we show that beyond this function, FKBP36 forms complexes with glyceraldehyde-3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) and Hsp90. Both proteins bind independently to different sites of the FKBP36 tetratricopeptide repeat domain. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH. In addition, FKBP36 expression causes a significant reduction of the GAPDH level and activity in COS-7 cells. Particularly in the cytosolic fraction, GAPDH was depleted by FKBP36 expression. Thus, FKBP36 diminishes GAPDH activity by direct interaction and down-regulation of GAPDH, which represents a previously unknown mechanism of GAPDH regulation and a novel function of FKBP36 in testis-specific signaling.

UI MeSH Term Description Entries
D008297 Male Males
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002522 Chlorocebus aethiops A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research. African Green Monkey,Cercopithecus aethiops,Cercopithecus griseoviridis,Cercopithecus griseus,Cercopithecus pygerythrus,Cercopithecus sabeus,Cercopithecus tantalus,Chlorocebus cynosuros,Chlorocebus cynosurus,Chlorocebus pygerythrus,Green Monkey,Grivet Monkey,Lasiopyga weidholzi,Malbrouck,Malbrouck Monkey,Monkey, African Green,Monkey, Green,Monkey, Grivet,Monkey, Vervet,Savanah Monkey,Vervet Monkey,Savannah Monkey,African Green Monkey,Chlorocebus cynosuro,Green Monkey, African,Green Monkeys,Grivet Monkeys,Malbrouck Monkeys,Malbroucks,Monkey, Malbrouck,Monkey, Savanah,Monkey, Savannah,Savannah Monkeys,Vervet Monkeys
D005987 Glyceraldehyde-3-Phosphate Dehydrogenases Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD. GAPD,Glyceraldehyde-3-Phosphate Dehydrogenase,Glyceraldehydephosphate Dehydrogenase,Phosphoglyceraldehyde Dehydrogenase,Triosephosphate Dehydrogenase,Dehydrogenase, Glyceraldehyde-3-Phosphate,Dehydrogenase, Glyceraldehydephosphate,Dehydrogenase, Phosphoglyceraldehyde,Dehydrogenase, Triosephosphate,Dehydrogenases, Glyceraldehyde-3-Phosphate,Glyceraldehyde 3 Phosphate Dehydrogenase
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D018841 HSP90 Heat-Shock Proteins A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS. Heat-Shock Proteins 90,HSP90 Heat Shock Proteins,Heat Shock Proteins 90,Heat-Shock Proteins, HSP90

Related Publications

Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
June 1981, Philosophical transactions of the Royal Society of London. Series B, Biological sciences,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
May 2006, The Journal of biological chemistry,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
June 2012, Biochemistry and cell biology = Biochimie et biologie cellulaire,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
September 1975, European journal of biochemistry,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
October 1959, The Journal of biological chemistry,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
January 2021, Biochimica et biophysica acta. Proteins and proteomics,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
June 1993, FEBS letters,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
January 2001, Bioorganic & medicinal chemistry letters,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
May 2020, Pharmaceutics,
Franziska Jarczowski, and Günther Jahreis, and Frank Erdmann, and Angelika Schierhorn, and Gunter Fischer, and Frank Edlich
August 1995, Biochemistry,
Copied contents to your clipboard!