title: Cytoplasmic domain of NCAM140 interacts with ubiquitin-fold modifier-conjugating enzyme-1 (Ufc1).
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.
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: mhomrich@uni-bonn.de.
authors.forename: Mirka
authors.initials: M
authors.lastname: Homrich
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: h.wobst@uni-bonn.de.
authors.forename: Hilke
authors.initials: H
authors.lastname: Wobst
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: claurini@uni-bonn.de.
authors.forename: Christine
authors.initials: C
authors.lastname: Laurini
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: julia.sab@gmx.de.
authors.forename: Julia
authors.initials: J
authors.lastname: Sabrowski
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: Schmitz@uni-bonn.de.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Schmitz
authors.affiliation: Institute of Nutrition and Food Science, Department of Human Metabolomics, University of Bonn, 53115 Bonn, Germany. Electronic address: s.diestel@uni-bonn.de.
authors.forename: Simone
authors.initials: S
authors.lastname: Diestel
mesh_terms: D000818:Animals; D019556:COS Cells; D015816:Cell Adhesion Molecules, Neuronal / Q000737:chemistry / Q000378:metabolism*; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000378:metabolism; D004705:Endocytosis / Q000235:genetics; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D040081:Protein Array Analysis; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000235:genetics; D011506:Proteins / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000737:chemistry / Q000378:metabolism*
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; C520249:NCAM140, human; D011506:Proteins; C502096:UFC1 protein, human; C502094:UFM1 protein, human; D044763:Ubiquitin-Conjugating Enzymes
keywords: Endocytosis; Neural cell adhesion molecule NCAM; Ubiquitin-fold modifier-1 (Ufm1); Ubiquitin-like proteins; Ufm1-conjugating enzyme-1 (Ufc1)