Proteomics Screen Identifies Class I Rab11 Family Interacting Proteins as Key Regulators of Cytokinesis. 2017

Carl Laflamme, and Jacob A Galan, and Khaled Ben El Kadhi, and Antoine Méant, and Carlos Zeledon, and Sébastien Carréno, and Philippe P Roux, and Gregory Emery
Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, Québec, Canada.

The 14-3-3 protein family orchestrates a complex network of molecular interactions that regulates various biological processes. Owing to their role in regulating the cell cycle and protein trafficking, 14-3-3 proteins are prevalent in human diseases such as cancer, diabetes, and neurodegeneration. 14-3-3 proteins are expressed in all eukaryotic cells, suggesting that they mediate their biological functions through evolutionarily conserved protein interactions. To identify these core 14-3-3 client proteins, we used an affinity-based proteomics approach to characterize and compare the human and Drosophila 14-3-3 interactomes. Using this approach, we identified a group of Rab11 effector proteins, termed class I Rab11 family interacting proteins (Rab11-FIPs), or Rip11 in Drosophila We found that 14-3-3 binds to Rip11 in a phospho-dependent manner to ensure its proper subcellular distribution during cell division. Our results indicate that Rip11 plays an essential role in the regulation of cytokinesis and that this function requires its association with 14-3-3 but not with Rab11. Together, our results suggest an evolutionarily conserved role for 14-3-3 in controlling Rip11-dependent protein transport during cytokinesis.

UI MeSH Term Description Entries
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D004330 Drosophila A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology. Fruit Fly, Drosophila,Drosophila Fruit Flies,Drosophila Fruit Fly,Drosophilas,Flies, Drosophila Fruit,Fly, Drosophila Fruit,Fruit Flies, Drosophila
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000072417 Protein Domains Discrete protein structural units that may fold independently of the rest of the protein and have their own functions. Peptide Domain,Protein Domain,Domain, Peptide,Domain, Protein,Domains, Peptide,Domains, Protein,Peptide Domains
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017124 Conserved Sequence A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences. Conserved Sequences,Sequence, Conserved,Sequences, Conserved
D048749 Cytokinesis The process by which the CYTOPLASM of a cell is divided. Cytoplasmic Division,Cytokineses,Cytoplasmic Divisions,Division, Cytoplasmic,Divisions, Cytoplasmic
D048948 14-3-3 Proteins A large family of signal-transducing adaptor proteins present in wide variety of eukaryotes. They are PHOSPHOSERINE and PHOSPHOTHREONINE binding proteins involved in important cellular processes including SIGNAL TRANSDUCTION; CELL CYCLE control; APOPTOSIS; and cellular stress responses. 14-3-3 proteins function by interacting with other signal-transducing proteins and effecting changes in their enzymatic activity and subcellular localization. The name 14-3-3 derives from numerical designations used in the original fractionation patterns of the proteins. 14-3-3 Protein,14-3-3 Protein, beta Isoform,14-3-3 Protein, epsilon Isoform,14-3-3 Protein, eta Isoform,14-3-3 Protein, gamma Isoform,14-3-3 Protein, tau Isoform,14-3-3 Protein, zeta Isoform,14-3-3 beta Protein,14-3-3 epsilon Protein,14-3-3 eta Protein,14-3-3 gamma Protein,14-3-3 tau Protein,14-3-3 zeta Protein,14-3-3beta Protein,14-3-3epsilon Protein,14-3-3eta Protein,14-3-3gamma Protein,14-3-3tau Protein,14-3-3zeta Protein,Brain 14-3-3 Protein,Protein 14-3-3,14 3 3 Protein,14 3 3 Protein, beta Isoform,14 3 3 Protein, epsilon Isoform,14 3 3 Protein, eta Isoform,14 3 3 Protein, gamma Isoform,14 3 3 Protein, tau Isoform,14 3 3 Protein, zeta Isoform,14 3 3 Proteins,14 3 3 beta Protein,14 3 3 epsilon Protein,14 3 3 eta Protein,14 3 3 gamma Protein,14 3 3 tau Protein,14 3 3 zeta Protein,14 3 3beta Protein,14 3 3epsilon Protein,14 3 3eta Protein,14 3 3gamma Protein,14 3 3tau Protein,14 3 3zeta Protein,14-3-3 Protein, Brain,Brain 14 3 3 Protein,Protein, 14-3-3tau,eta Protein, 14-3-3

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