8S6O

Structure of MLLE3 domain of Rrm4 in complex with PAM2L2 of Upa1

Summary for 8S6O

• Entry DOI: 10.2210/pdb8s6o/pdb
• Related: 8S6N
• Descriptor: RNA-binding protein RRM4, PAMPL2 (3 entities in total)
• Functional Keywords: rna transport ustilago maydis, rna
• Biological source: Ustilago maydis; More
• Total number of polymer chains: 16
• Total formula weight: 121611.62

Authors

Devan, S.,Shanmugasundaram, S.,Muentjes, K.,Smits, S.H.,Altegoer, F.,Feldbruegge, M. (deposition date: 2024-02-28, release date: 2024-10-30, Last modification date: 2024-11-20)

Primary citation

Devan, S.K.,Shanmugasundaram, S.,Muntjes, K.,Postma, J.,Smits, S.H.J.,Altegoer, F.,Feldbrugge, M.
Deciphering the RNA-binding protein network during endosomal mRNA transport.
Proc.Natl.Acad.Sci.USA, 121:e2404091121-e2404091121, 2024

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

PubMed: 39499630
DOI: 10.1073/pnas.2404091121

Experimental method

X-RAY DIFFRACTION (2.4 Å)