Proteomics

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Mechanism of 60S ribosomal subunit recognition and UFMylation by the UFM1 E3 ligase complex

ABSTRACT: 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.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Calabrese  

LAB HEAD: Antonio Calabrese

PROVIDER: PXD046990 | Pride | 2024-03-22

REPOSITORIES: Pride

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Action DRS
23089_Anton_Ecl_DSBU_XL_TRAP_50cm_90min_Dundee_1.pdResult Other
23089_Anton_Ecl_DSBU_XL_TRAP_50cm_90min_Dundee_1.raw Raw
23089_Anton_Ecl_DSBU_XL_TRAP_50cm_90min_Dundee_2.pdResult Other
23089_Anton_Ecl_DSBU_XL_TRAP_50cm_90min_Dundee_2.raw Raw
fbstcm_220922_04_RiboE3_XL.pdResult Other
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Publications

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]

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