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20 results on '"Olkkonen, Vesa M"'

1. A microRNA Cluster Controls Fat Cell Differentiation and Adipose Tissue Expansion By Regulating SNCG

Author

Rodríguez‐Barrueco, Ruth, primary, Latorre, Jessica, additional, Devis‐Jáuregui, Laura, additional, Lluch, Aina, additional, Bonifaci, Nuria, additional, Llobet, Francisco J., additional, Olivan, Mireia, additional, Coll‐Iglesias, Laura, additional, Gassner, Katja, additional, Davis, Meredith L., additional, Moreno‐Navarrete, José M., additional, Castells‐Nobau, Anna, additional, Plata‐Peña, Laura, additional, Dalmau‐Pastor, Miki, additional, Höring, Marcus, additional, Liebisch, Gerhard, additional, Olkkonen, Vesa M., additional, Arnoriaga‐Rodríguez, Maria, additional, Ricart, Wifredo, additional, Fernández‐Real, José M., additional, Silva, José M., additional, Ortega, Francisco J., additional, and Llobet‐Navas, David, additional

Published
2021
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2. ORP2, a cholesterol transporter, regulates angiogenic signaling in endothelial cells

Author

Koponen, Annika, primary, Pan, Guoping, additional, Kivelä, Annukka M., additional, Ralko, Arthur, additional, Taskinen, Juuso H., additional, Arora, Amita, additional, Kosonen, Riikka, additional, Kari, Otto K., additional, Ndika, Joseph, additional, Ikonen, Elina, additional, Cho, Wonhwa, additional, Yan, Daoguang, additional, and Olkkonen, Vesa M., additional

Published
2020
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3. The PNPLA3‐I148M variant increases polyunsaturated triglycerides in human adipose tissue

Author

Qadri, Sami, primary, Lallukka‐Brück, Susanna, additional, Luukkonen, Panu K., additional, Zhou, You, additional, Gastaldelli, Amalia, additional, Orho‐Melander, Marju, additional, Sammalkorpi, Henna, additional, Juuti, Anne, additional, Penttilä, Anne K., additional, Perttilä, Julia, additional, Hakkarainen, Antti, additional, Lehtimäki, Tiina E., additional, Orešič, Matej, additional, Hyötyläinen, Tuulia, additional, Hodson, Leanne, additional, Olkkonen, Vesa M., additional, and Yki‐Järvinen, Hannele, additional

Published
2020
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6. Novel hepatic microRNAs upregulated in human nonalcoholic fatty liver disease

Author

Soronen, Jarkko, primary, Yki-Järvinen, Hannele, additional, Zhou, You, additional, Sädevirta, Sanja, additional, Sarin, Antti-Pekka, additional, Leivonen, Marja, additional, Sevastianova, Ksenia, additional, Perttilä, Julia, additional, Laurila, Pirkka-Pekka, additional, Sigruener, Alexander, additional, Schmitz, Gerd, additional, and Olkkonen, Vesa M., additional

Published
2016
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19. The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/SNAP-25.

Author

Weber-Boyvat M, Chernov KG, Aro N, Wohlfahrt G, Olkkonen VM, and Jäntti J

Subjects
Animals, Cell Line, Cell Membrane metabolism, Fungal Proteins genetics, Fungal Proteins metabolism, Humans, Membrane Fusion physiology, Munc18 Proteins genetics, Mutation genetics, Protein Binding physiology, Synaptosomal-Associated Protein 25 genetics, Yeasts genetics, Yeasts metabolism, Munc18 Proteins metabolism, Synaptosomal-Associated Protein 25 metabolism
Abstract

The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNARE-mediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here, we show that a sec1 groove mutant yeast strain, sec1(w24), displays temperature-sensitive growth and secretion defects. The yeast Sec1p and mammalian Munc18-1 grooves were shown to play an important role in the interaction with the SNAREs Sec9p and SNAP-25b, respectively. Incubation of SNAP-25b with the Munc18-1 groove mutant resulted in a lag in the kinetics of SNARE complex assembly in vitro when compared with wild-type Munc18-1. The SNARE regulator SRO7 was identified as a multicopy suppressor of sec1(w24) groove mutant and an intact Sec1p groove was required for the plasma membrane targeting of Sro7p-SNARE complexes. Simultaneous inactivation of Sec1p groove and SRO7 resulted in reduced levels of exocytic SNARE complexes. Our results identify the groove as a conserved interaction surface in SM proteins. The results indicate that this structural element is important for interactions with Sec9p/SNAP-25 and participates, in concert with Sro7p, in the initial steps of SNARE complex assembly., (© 2015 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.)

Published
2016
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20. Role of ORPs in sterol transport from plasma membrane to ER and lipid droplets in mammalian cells.

Author

Jansen M, Ohsaki Y, Rega LR, Bittman R, Olkkonen VM, and Ikonen E

Subjects
Amino Acid Motifs, Biological Transport, Carrier Proteins genetics, Carrier Proteins metabolism, Cell Line, Tumor, Cell Membrane genetics, Cholesterol metabolism, Gene Knockdown Techniques, HeLa Cells, Humans, Protein Binding, Protein Structure, Tertiary, Receptors, Steroid genetics, Structure-Activity Relationship, Vesicular Transport Proteins genetics, Vesicular Transport Proteins metabolism, Cell Membrane metabolism, Endoplasmic Reticulum metabolism, Lipid Metabolism physiology, Receptors, Steroid metabolism, Sterols metabolism
Abstract

In this study, we investigated the mechanisms of sterol transport from the plasma membrane (PM) to the endoplasmic reticulum (ER) and lipid droplets (LDs) in HeLa cells. By overexpressing all mammalian oxysterol-binding protein-related proteins (ORPs), we found that especially ORP1S and ORP2 enhanced PM-to-LD sterol transport. This reflected the stimulation of transport from the PM to the ER, rather than from the ER to LDs. Double knockdown of ORP1S and ORP2 inhibited sterol transport from the PM to the ER and LDs, suggesting a physiological role for these ORPs in the process. A two phenylalanines in an acidic tract (FFAT) motif in ORPs that mediates interaction with VAMP-associated proteins (VAPs) in the ER was not necessary for the enhancement of sterol transport by ORPs. However, VAP-A and VAP-B silencing slowed down PM-to-LD sterol transport. This was accompanied by enhanced degradation of ORP2 and decreased levels of several FFAT motif-containing ORPs, suggesting a role for VAPs in sterol transport by stabilization of ORPs., (© 2010 John Wiley & Sons A/S.)

Published
2011
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