Specificity of transmembrane protein palmitoylation in yeast.

Autor: Ayelén González Montoro, Sabrina Chumpen Ramirez, Rodrigo Quiroga, Javier Valdez Taubas

Publikováno v: PLoS ONE, Vol 6, Iss 2, p e16969 (2011)

Many proteins are modified after their synthesis, by the addition of a lipid molecule to one or more cysteine residues, through a thioester bond. This modification is called S-acylation, and more commonly palmitoylation. This reaction is carried out

Externí odkaz: https://doaj.org/article/40440d4b4fb7409587a63634273c107a

Multiple tethers of organelle contact sites are involved in α-synuclein toxicity in yeast

Autor: Mara Del Vecchio, Lucia Amado, Alexandra P. Cogan, Els Meert, Joelle Rosseels, Vanessa Franssens, Sander K. Govers, Joris Winderickx, Ayelén González Montoro

Publikováno v: Molecular Biology of the Cell.

The protein alpha-synuclein (α-syn) is one of the major factors linked to Parkinson's disease, yet how its misfolding and deposition contribute to the pathology remains largely elusive. Recently, contact sites among organelles were implicated in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::889ce390b2db2187dab37ff8cdef8d4e
https://doi.org/10.1091/mbc.e23-01-0029

The yeast LYST homolog Bph1 is a Rab5 effector and prevents Atg8 lipidation at endosomes

Autor: Prado Vargas Duarte, Ralph Hardenberg, Muriel Mari, Stefan Walter, Fulvio Reggiori, Florian Fröhlich, Ayelén González Montoro, Christian Ungermann

Publikováno v: Journal of Cell Science, 135(8). COMPANY OF BIOLOGISTS LTD

Lysosomes mediate degradation of macromolecules to their precursors for cellular recycling. Additionally, lysosome-related organelles mediate cell type-specific functions. Chédiak–Higashi syndrome is an autosomal, recessive disease, in which loss

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5820e9dc5e18dbfb45ea51deeb3c31f
https://doi.org/10.1242/jcs.259421

The receptor subunit Tom20 is dynamically associated with the TOM complex in mitochondria of human cells

Autor: Niklas Webeling, Maniraj Bhagawati, Karin B. Busch, Henning D. Mootz, Ayelén González Montoro, Tasnim Arroum

Publikováno v: Molecular Biology of the Cell

The outer membrane translocase (TOM) is the import channel for nuclear-encoded mitochondrial proteins. The general import pore contains Tom40, Tom22, Tom5, Tom6, and Tom7. Precursor proteins are bound by the (peripheral) receptor proteins Tom20, Tom2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2297ae76ce9cbb8820493cc7fceb4ba0
https://pubmed.ncbi.nlm.nih.gov/34347503

Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites

Autor: Florian Fröhlich, Martin van der Laan, Christian Ungermann, Thomas Becker, Carina Hönscher, Fulvio Reggiori, Kathrin Auffarth, Ayelén González Montoro, Bettina Warscheid, Maria Bohnert

Publikováno v: Developmental Cell
Developmental Cell, 45(5), 621-636.e7. CELL PRESS
González Montoro, A, Auffarth, K, Hönscher, C, Bohnert, M, Becker, T, Warscheid, B, Reggiori, F, van der Laan, M, Fröhlich, F & Ungermann, C 2018, ' Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites ', Developmental Cell, vol. 45, no. 5, pp. 621-636.e7 . https://doi.org/10.1016/j.devcel.2018.05.011

The extensive subcellular network of membrane contact sites plays central roles in organelle biogenesis and communication, yet the precise contributions of the involved machineries remain largely enigmatic. The yeast vacuole forms a membrane contact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17b4e1d3bd43918d885926515c7332b9
https://pubmed.ncbi.nlm.nih.gov/29870720