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 Lettjournal_title
FEBS lettersauthors
Garcia-Gonzalo FR,Cruz C,Muñoz P,Mazurek S,Eigenbrodt E,Ventura F,Bartrons R,Rosa JLdoi
10.1016/s0014-5793(03)00205-9keywords:
subject
Has Abstractpub_date
2003-03-27 00:00:00pages
78-84issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579303002059journal_volume
539pub_type
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