UFM1 ribosome E3 ligase complex bound to the 60S ribosomal subunit
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ABSTRACT:
SUBMITTER: Linda Makhlouf
PROVIDER: EMPIAR-11906 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons.
Makhlouf Linda L Peter Joshua J JJ Magnussen Helge M HM Thakur Rohan R Millrine David D Minshull Thomas C TC Harrison Grace G Varghese Joby J Lamoliatte Frederic F Foglizzo Martina M Macartney Thomas T Calabrese Antonio N AN Zeqiraj Elton E Kulathu Yogesh Y
Nature 20240221 8003
Stalled ribosomes at the endoplasmic reticulum (ER) are covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 (also known as uL24)<sup>1,2</sup>. This modification, which is known as UFMylation, is orchestrated by the UFM1 ribosome E3 ligase (UREL) complex, comprising UFL1, UFBP1 and CDK5RAP3 (ref. <sup>3</sup>). However, the catalytic mechanism of UREL and the functional consequences of UFMylation are unclear. Here we present cryo-electron microscop ...[more]
Similar Datasets
Project description:During co-translational translocation at the endoplasmic reticulum (ER), ribosomes can stall and become covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit RPL26 (uL24). This process, known as UFMylation, is mediated by the UFM1 Ribosome E3 Ligase (UREL) complex, comprised of UFL1, UFBP1, and CDK5RAP3. However, the functional consequences of UFMylation and catalytic mechanisms of UREL are unknown. Here, we present crosslinking-mass spectrometry (XL-MS) data of UREL bound to 60S ribosomes.
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2015-06-13 | E-GEOD-69826 | biostudies-arrayexpress
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