Deciphering the RNA-binding protein network during endosomal mRNA transport DOI Creative Commons
Senthil-Kumar Devan,

Sainath Shanmugasundaram,

Kira Müntjes

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: March 23, 2024

Abstract Microtubule-dependent endosomal transport is crucial for polar growth, ensuring the precise distribution of cellular cargos such as proteins and mRNAs. However, molecular mechanism linking mRNAs to surface remains poorly understood. Here, we present a structural analysis key RNA-binding protein Rrm4 from Ustilago maydis . Our findings reveal new type MademoiseLLE domain featuring seven-helical bundle that provides distinct binding interface. A comparative with canonical MLLE poly(A)-binding Pab1 disclosed unique characteristics both domains. Deciphering code enabled prediction verification previously unknown interactors containing short linear motifs. Importantly, demonstrated human domains, those PABPC1 UBR5, employed similar principle distinguish among interaction partners. Thus, our study unprecedented mechanistic insights into how variations in widely distributed facilitates mRNA attachment during transport. Significance Polar growing cells, fungal hyphae neurons, utilize endosomes along their microtubules. But do these precisely attach endosomes? addresses this question by investing transporter, Rrm4, model microorganism. We uncovered features protein-protein recognizes specific motifs While resembles one found protein, it exhibits motif recognition. underlying unveiled partners Rrm4. The recognition system used form resilient network (RBPs) This applicable humans, highlighting its fundamental importance.

Language: Английский

Deciphering the RNA-binding protein network during endosomal mRNA transport DOI Creative Commons
Senthil-Kumar Devan,

Sainath Shanmugasundaram,

Kira Müntjes

et al.

Proceedings of the National Academy of Sciences, Journal Year: 2024, Volume and Issue: 121(46)

Published: Nov. 5, 2024

Microtubule-dependent endosomal transport is crucial for polar growth, ensuring the precise distribution of cellular cargos such as proteins and mRNAs. However, molecular mechanism linking mRNAs to surface remains poorly understood. Here, we present a structural analysis key RNA-binding protein Rrm4 from Ustilago maydis . Our findings reveal different type MademoiseLLE domain (MLLE) featuring seven-helical bundle that provides distinct binding interface. A comparative with canonical poly(A)-binding Pab1 disclosed unique characteristics both domains. Deciphering MLLE code enabled prediction verification previously unknown interactors containing short linear motifs. Importantly, demonstrated human domains, those PABPC1 UBR5, employed similar principle distinguish among interaction partners. Thus, our study detailed mechanistic insights into how variations in widely distributed facilitate mRNA attachment during transport.

Language: Английский

Citations

1
Deciphering the RNA-binding protein network during endosomal mRNA transport DOI Creative Commons
Senthil-Kumar Devan,

Sainath Shanmugasundaram,

Kira Müntjes

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: March 23, 2024

Abstract Microtubule-dependent endosomal transport is crucial for polar growth, ensuring the precise distribution of cellular cargos such as proteins and mRNAs. However, molecular mechanism linking mRNAs to surface remains poorly understood. Here, we present a structural analysis key RNA-binding protein Rrm4 from Ustilago maydis . Our findings reveal new type MademoiseLLE domain featuring seven-helical bundle that provides distinct binding interface. A comparative with canonical MLLE poly(A)-binding Pab1 disclosed unique characteristics both domains. Deciphering code enabled prediction verification previously unknown interactors containing short linear motifs. Importantly, demonstrated human domains, those PABPC1 UBR5, employed similar principle distinguish among interaction partners. Thus, our study unprecedented mechanistic insights into how variations in widely distributed facilitates mRNA attachment during transport. Significance Polar growing cells, fungal hyphae neurons, utilize endosomes along their microtubules. But do these precisely attach endosomes? addresses this question by investing transporter, Rrm4, model microorganism. We uncovered features protein-protein recognizes specific motifs While resembles one found protein, it exhibits motif recognition. underlying unveiled partners Rrm4. The recognition system used form resilient network (RBPs) This applicable humans, highlighting its fundamental importance.

Language: Английский

Citations

0