Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Marius K Lemberg"'
Autor:
Verena Dederer, Anton Khmelinskii, Anna Gesine Huhn, Voytek Okreglak, Michael Knop, Marius K Lemberg
Publikováno v:
eLife, Vol 8 (2019)
Tail-anchored (TA) proteins insert post-translationally into the endoplasmic reticulum (ER), the outer mitochondrial membrane (OMM) and peroxisomes. Whereas the GET pathway controls ER-targeting, no dedicated factors are known for OMM insertion, posi
Externí odkaz:
https://doaj.org/article/c6f8f3892e2d41028bef137849c62e07
Autor:
Julia D. Knopf, Susanne S. Steigleder, Friederike Korn, Nathalie Kühnle, Marina Badenes, Marina Tauber, Sebastian J. Theobald, Jan Rybniker, Colin Adrain, Marius K. Lemberg
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The toll-like receptor 4 (TLR4) is a central regulator of innate immunity that primarily recognizes bacterial lipopolysaccharide cell wall constituents to trigger cytokine secretion. We identify the intramembrane protease RHBDL4 as a negativ
Externí odkaz:
https://doaj.org/article/2af17f35039c4574bcf982ab43936405
Autor:
Sara Suna Yücel, Walter Stelzer, Alessandra Lorenzoni, Manfred Wozny, Dieter Langosch, Marius K. Lemberg
Publikováno v:
Cell Reports, Vol 26, Iss 11, Pp 3087-3099.e11 (2019)
Summary: Unspliced XBP1 mRNA encodes XBP1u, the transcriptionally inert variant of the unfolded protein response (UPR) transcription factor XBP1s. XBP1u targets its mRNA-ribosome-nascent-chain-complex to the endoplasmic reticulum (ER) to facilitate U
Externí odkaz:
https://doaj.org/article/60d8072ac21a442c9cfc6d10165dcdc1
Autor:
Verena Dederer, Marius K. Lemberg
Publikováno v:
Trends in Cell Biology. 31:898-911
Precise distribution of proteins is essential to sustain the viability of cells. A complex network of protein synthesis and targeting factors cooperate with protein quality control systems to ensure protein homeostasis. Defective proteins are inevita
Autor:
Edita Poláchová, Kathrin Bach, Elena Heuten, Stancho Stanchev, Anežka Tichá, Philipp Lampe, Pavel Majer, Thomas Langer, Marius K. Lemberg, Kvido Stříšovský
Publikováno v:
Journal of medicinal chemistry.
The mitochondrial rhomboid protease PARL regulates mitophagy by balancing intramembrane proteolysis of PINK1 and PGAM5. It has been implicated in the pathogenesis of Parkinson's disease, but its investigation as a possible therapeutic target is chall
Autor:
Andrea Zanotti, João P. L. Coelho, Dinah Kaylani, Gurdeep Singh, Marina Tauber, Manuel Hitzenberger, Dönem Avci, Martin Zacharias, Robert B. Russell, Marius K. Lemberg, Matthias J. Feige
Publikováno v:
Science (New York, N.Y.). 378(6623)
Cells need to detect and degrade faulty membrane proteins to maintain homeostasis. In this study, we identify a previously unknown function of the human signal peptidase complex (SPC)—the enzyme that removes endoplasmic reticulum (ER) signal peptid
Autor:
Oskar Engberg, David Ulbricht, Viola Döbel, Verena Siebert, Christian Frie, Anja Penk, Marius K. Lemberg, Daniel Huster
Publikováno v:
Science advances. 8(38)
Membrane thinning by rhomboid proteins has been proposed to reduce hydrophobic mismatch, providing a unique environment for important functions ranging from intramembrane proteolysis to retrotranslocation in protein degradation. We show by in vitro r
Autor:
Marius K. Lemberg, Kvido Strisovsky
Publikováno v:
Molecular Cell. 81:2507-2519
Protein homeostasis mechanisms are fundamentally important to match cellular needs and to counteract stress conditions. A fundamental challenge is to understand how defective proteins are recognized and extracted from cellular organelles to be degrad
Autor:
Marius K. Lemberg, Sara Suna Yucel
Publikováno v:
Journal of Molecular Biology. 432:5063-5078
Intramembrane proteases catalyze the unusual cleavage of peptide bonds in the plane of biological membranes. They are categorized according to their active site. The GxGD aspartyl proteases comprise presenilin, the signal peptide peptidase (SPP), and
The intramembrane protease PARL is a crucial mitochondrial safeguard by cleaving the mitophagy regulators PINK1 and PGAM5. PGAM5 substrate determinates have not been rigorously investigated and it is unclear how uncoupling the mitochondrial membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ff7ef1d45387920e8cf99c460ff5e2e
https://doi.org/10.1101/2021.11.19.469224
https://doi.org/10.1101/2021.11.19.469224