Interaction between HERC1 and M2-type pyruvate kinase.
HERC proteins are characterized by having one or more RCC1-like domains as well as a C-terminal HECT domain in their amino acid sequences. This has led researchers to suggest that they may act as both guanine nucleotide exchange factors and E3 ubiquitin ligases. Here we describe a physical interaction between the HECT domain of HERC1, a giant protein involved in intracellular membrane traffic, and the M2 isoform of glycolytic enzyme pyruvate kinase (M2-PK). Partial colocalization of endogenous proteins was observed by immunofluorescence studies. This interaction neither induced M2-PK ubiquitination nor affected its enzymatic activity. The putative significance of the association is discussed.
Garcia-Gonzalo
Francesc R
FR
Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, C/Feixa Llarga s/n, L'Hospitalet de Llobregat, E-08907 Barcelona, Spain.
Cruz
Cristina
C
Muñoz
Purificación
P
Mazurek
Sybille
S
Eigenbrodt
Erich
E
Ventura
Francesc
F
Bartrons
Ramon
R
Rosa
Jose Luis
JL
D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D006367:HeLa Cells; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; C468925:ERC1 protein, human; D009419:Nerve Tissue Proteins; D011770:Pyruvate Kinase