Efficient protein trafficking requires trailer hitch, a component of a ribonucleoprotein complex localized to the ER in Drosophila

James E. Wilhelm, Michael Buszczak, Suzanne Sayles

Research output: Contribution to journalArticle

119 Citations (Scopus)

Abstract

Translational control of localized messenger mRNAs (mRNAs) is critical for cell polarity, synaptic plasticity, and embryonic patterning. While progress has been made in identifying localization factors and translational regulators, it is unclear how broad a role they play in regulating basic cellular processes. We have identified Drosophila trailer hitch (tral) as a gene that is required for the proper secretion of the dorsal-ventral patterning factor Gurken, as well as the vitellogenin receptor Yolkless. Surprisingly, biochemical purification of Tral revealed that it is part of a large RNA-protein complex that includes the translation/localization factors Me31B and Cup as well as the mRNAs for endoplasmic reticulum (ER) exit site components. This complex is localized to subdomains of the ER that border ER exit sites. Furthermore, tral is required for normal ER exit site formation. These findings raise exciting new possibilities for how the mRNA localization machinery could interface with the classical secretory pathway to promote efficient protein trafficking in the cell.

Original languageEnglish (US)
Pages (from-to)675-685
Number of pages11
JournalDevelopmental Cell
Volume9
Issue number5
DOIs
StatePublished - Nov 2005

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Ribonucleoproteins
Light trailers
Protein Transport
Endoplasmic Reticulum
Drosophila
Messenger RNA
Proteins
Cell Polarity
Neuronal Plasticity
Secretory Pathway
Machinery
Purification
Plasticity
Genes
RNA

ASJC Scopus subject areas

  • Developmental Biology

Cite this

Efficient protein trafficking requires trailer hitch, a component of a ribonucleoprotein complex localized to the ER in Drosophila. / Wilhelm, James E.; Buszczak, Michael; Sayles, Suzanne.

In: Developmental Cell, Vol. 9, No. 5, 11.2005, p. 675-685.

Research output: Contribution to journalArticle

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