Interaction between HERC1 and M2-type pyruvate kinase.

Francesc R Garcia-Gonzalo; Cristina Cruz; Purificación Muñoz; Sybille Mazurek; Erich Eigenbrodt; Francesc Ventura; Ramon Bartrons; Jose Luis Rosa

doi:10.1016/s0014-5793(03)00205-9

PubMed · 12650930

Interaction between HERC1 and M2-type pyruvate kinase.

Francesc R Garcia-Gonzalo·Cristina Cruz·Purificación Muñoz·Sybille Mazurek·Erich Eigenbrodt·Francesc Ventura·Ramon Bartrons·Jose Luis Rosa

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Abstract

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.

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Adaptor Proteins, Signal Transducing Carrier Proteins Cell Line HeLa Cells Humans Nerve Tissue Proteins Pyruvate Kinase Two-Hybrid System Techniques Journal Article Research Support, Non-U.S. Gov't

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Francesc R Garcia-Gonzalo, Cristina Cruz, Purificación Muñoz, Sybille Mazurek, Erich Eigenbrodt, Francesc Ventura, Ramon Bartrons, Jose Luis Rosa. 2003-03-27. Interaction between HERC1 and M2-type pyruvate kinase.. https://doi.org/10.1016/s0014-5793(03)00205-9

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