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Cited by 30RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

HDLBP binds ER-targeted mRNAs by multivalent interactions to promote protein synthesis of transmembrane and secreted proteins

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Zinnall, Ulrike, Milek, Miha, Minia, Igor, Vieira-Vieira, Carlos H., Müller, Simon, Mastrobuoni, Guido, Hazapis, Orsalia-Georgia, Del Giudice, Simone +8 more·2022·Nature Communications
DOI 10.1038/s41467-022-30322-7PMC PMC9117268
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Abstract

The biological role of RNA-binding proteins in the secretory pathway is not well established. Here, we describe that human HDLBP/Vigilin directly interacts with more than 80% of ER-localized mRNAs. PAR-CLIP analysis reveals that these transcripts represent high affinity HDLBP substrates and are specifically bound in their coding sequences (CDS), in contrast to CDS/3’UTR-bound cytosolic mRNAs. HDLBP crosslinks strongly to long CU-rich motifs, which frequently reside in CDS of ER-localized mRNAs and result in high affinity multivalent interactions. In addition to HDLBP-ncRNA interactome, quantification of HDLBP-proximal proteome confirms association with components of the translational apparatus and the signal recognition particle. Absence of HDLBP results in decreased translation efficiency of HDLBP target mRNAs, impaired protein synthesis and secretion in model cell lines, as well as decreased tumor growth in a lung cancer mouse model. These results highlight a general function for HDLBP in the translation of ER-localized mRNAs and its relevance for tumor progression.

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  • HDLBP is a candidate with known effects on secretory processes including VLDL secretion.

    “A promising target from this analysis was high density lipoprotein binding protein (HDLBP), a candidate with known effects on secretory processes including VLDL secretion (14, 15).”

    From Loss of function of T-box 3 in the liver protects against MASLD (2025) · cites this paper as [15]

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References 95 · Cited by 30

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Authors
Zinnall, U., Milek, M., Minia, I., Vieira-Vieira, C. H., Müller, S., Mastrobuoni, G., Hazapis, O.-G., Del Giudice, S., Schwefel, D., Bley, N., Voigt, F., Chao, J. A., Kempa, S., Hüttelmaier, S., Selbach, M., & Landthaler, M.
Affiliations
  • Max Delbrück Center (DE)
  • Martin Luther University Halle-Wittenberg (DE)
  • Humboldt-Universität zu Berlin (DE)
  • Friedrich Miescher Institute (CH)
Corresponding author
  • Milek, Miha
  • Landthaler, Markus
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2022-05-18
Volume
13
Issue
1
Pages
2727-2727
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-022-30322-7
PMC
PMC9117268
OpenAlex
W4280551763
Cited by
30
References
95
Citations by year
2026: 9 · 2025: 8 · 2024: 8 · 2023: 3 · 2022: 2
FWCI
1.71
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (submittedVersion, other-oa)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Deutsche Forschungsgemeinschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Keywords
vigilin, RNA-binding proteins, signal recognition particle, translation efficiency, secretory pathway, secreted proteins, tumor growth, lung cancer, PAR-CLIP
MeSH terms
Animals, Cell Line, Cytosol, Endoplasmic Reticulum, Humans, Membrane Proteins, RNA, Messenger, Protein Biosynthesis, RNA-Binding Proteins, Signal Recognition Particle, 3' Untranslated Regions, Mice

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