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Autor:
Douglas R. Green, Ricardo Weinlich
Publikováno v:
Molecular Cell. 56(4):469-480
Receptor Interacting Protein Kinase-1 (RIPK1), a key player in inflammation and cell death, assumes opposite functions depending on the cellular context and its posttranslational modifications. Genetic evidence supported by biochemical and cellular b
Autor:
J. Wade Harper, Tiao Xie, Alban Ordureau, Sean A. Beausoleil, James T. Koerber, Vladislav O. Sviderskiy, Steven P. Gygi, Shireen A. Sarraf, Jin-Mi Heo, James A. Wells, Jennifer L. Olszewski, Brenda A. Schulman, Mark P. Jedrychowski, David M. Duda
Publikováno v:
Molecular cell, vol 56, iss 3
Summary Phosphorylation is often used to promote protein ubiquitylation, yet we rarely understand quantitatively how ligase activation and ubiquitin (UB) chain assembly are integrated with phosphoregulation. Here we employ quantitative proteomics and
Autor:
Seong Won Lee, Chin Ha Chung, Seung Hyeun Ka, Hee Min Yoo, Dong Young Noh, Keiji Tanaka, Joo-Eun Lee, Young Joo Jeon, Jae Yeon Kim, Masaaki Komatsu, Yu-shin Sou, Sung Hwan Kang, Min Woo Seong, Soon-Tae Lee, Sung Hee Baek
Publikováno v:
Molecular Cell. 56:261-274
Biological roles for UFM1, a ubiquitin-like protein, are largely unknown, and therefore we screened for targets of ufmylation. Here we show that ufmylation of the nuclear receptor coactivator ASC1 is a key step for ERα transactivation in response to
Autor:
Wen-Xing Ding, Zhixun Dou, Ya Ping Jiang, Jorge Moscat, Nadia Jaber, Maria T. Diaz-Meco, Alex J. Bott, Joseph M. Catanzaro, Juei Suei Chen, Yu Sun, Chunying Du, Richard Z. Lin, Wei-Xing Zong, Bin Yang, Keiko Ozato, Ji-An Pan
Publikováno v:
Molecular Cell. 62:149-151
TRIM21 is a RING finger domain-containing ubiquitin E3 ligase whose expression is elevated in autoimmune disease. While TRIM21 plays an important role in immune activation during pathogen infection, little is known about its inherent cellular functio
Autor:
Larissa A. Canadeo, Jon M. Huibregtse
Publikováno v:
Molecular Cell. 62:2-4
HECT-family E3 ligases ubiquitinate protein substrates to control virtually every eukaryotic process, and are misregulated in numerous diseases. Nonetheless, understanding of HECT E3s is limited by a paucity of selective and potent modulators. To ove
Autor:
Johannes van den Boom, Hemmo Meyer
Publikováno v:
Molecular cell. 69(2)
The AAA+-type ATPase p97 governs an ever-expanding number of cellular processes reaching from degradation of damaged proteins and organelles to key signaling events and chromatin regulation with thousands of client proteins. With its relevance for ce
Publikováno v:
Molecular cell. 69(1)
The cytosolic iron-sulfur (Fe-S) cluster assembly (CIA) pathway functions to incorporate inorganic Fe-S cofactors into a variety of proteins, including several DNA repair enzymes. However, the mechanisms regulating the CIA pathway are unknown. We des
Autor:
Xiaolan Zhao, Nalini Dhingra
Publikováno v:
Molecular cell. 66(5)
In this issue of Molecular Cell, Wei et al. (2017) report how a DNA translocase uses SUMO as a cue to save Top2 from ubiquitin-mediated degradation and to minimize DNA breaks, thus providing insights into the SUMO and ubiquitin interplay in genome ma
Autor:
Mads Gyrd-Hansen, Matous Hrdinka
Publikováno v:
Molecular cell. 68(2)
The linear ubiquitin chain assembly complex, LUBAC, is the only known mammalian ubiquitin ligase that makes methionine 1 (Met1)-linked polyubiquitin (also referred to as linear ubiquitin). A decade after LUBAC was discovered as a cellular activity of
Publikováno v:
Molecular cell. 68(2)
Summary Tetherin (BST2/CD317) is an interferon-inducible antiviral factor known for its ability to block the release of enveloped viruses from infected cells. Yet its role in type I interferon (IFN) signaling remains poorly defined. Here, we demonstr