Cytoplasmic domain of NCAM140 interacts with ubiquitin-fold modifier-conjugating enzyme-1 (Ufc1) |
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| Authors: | Mirka Homrich Hilke Wobst Christine Laurini Julia Sabrowski Brigitte Schmitz Simone Diestel |
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| Affiliation: | Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany |
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| Abstract: | The neural cell adhesion molecule NCAM is implicated in different neurodevelopmental processes and in synaptic plasticity in adult brain. The cytoplasmic domain of NCAM interacts with several cytoskeletal proteins and signaling molecules. To identify novel interaction partners of the cytosolic domain of NCAM a protein macroarray has been performed. We identified the ubiquitin-fold modifier-conjugating enzyme-1 (Ufc1) as an interaction partner of NCAM140. Ufc1 is one of the enzymes involved in modification of proteins with the ubiquitin-like molecule ubiquitin-fold modifier-1 (Ufm1). We also observed a partial co-localization of NCAM140 with Ufc1 and Ufm1 and increased endocytosis of NCAM140 in the presence of Ufm1 suggesting a possible ufmylation of NCAM140 and a potential novel function of Ufm1 for cell surface proteins. |
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| Keywords: | ABTS, 2,2&prime -Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) cyt, Cytosolic tail GAP, Growth associated protein GST, Glutathione S-transferase LANP, Leucine-rich acidic nuclear protein NCAM, Neural cell adhesion molecule POD, Peroxidase PLC, Protein lipase C PP, Protein phosphatase TOAD, Turned on after division UBL, Ubiquitin-like protein Ufc1, Ubiquitin-fold modifier-conjugating enzyme-1 Ufm1, Ubiquitin-fold modifier-1 Ufl1, Ufm1-specific ligase 1 wt, Wild type |
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