Interaction between HERC1 and M2-type pyruvate kinase.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Garcia-Gonzalo FR,Cruz C,Muñoz P,Mazurek S,Eigenbrodt E,Ventura F,Bartrons R,Rosa JL

doi

10.1016/s0014-5793(03)00205-9

keywords:

subject

Has Abstract

pub_date

2003-03-27 00:00:00

pages

78-84

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579303002059

journal_volume

539

pub_type

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