Sumoylation in axons triggers retrograde transport of the RNA-binding protein La. Academic Article uri icon

Overview

abstract

  • A surprisingly large population of mRNAs has been shown to localize to sensory axons, but few RNA-binding proteins have been detected in these axons. These axonal mRNAs include several potential binding targets for the La RNA chaperone protein. La is transported into axonal processes in both culture and peripheral nerve. Interestingly, La is posttranslationally modified in sensory neurons by sumoylation. In axons, small ubiquitin-like modifying polypeptides (SUMO)-La interacts with dynein, whereas native La interacts with kinesin. Lysine 41 is required for sumoylation, and sumoylation-incompetent La(K41R) shows only anterograde transport, whereas WT La shows both anterograde and retrograde transport in axons. Thus, sumoylation of La determines the directionality of its transport within the axonal compartment, with SUMO-La likely recycling to the cell body.

publication date

  • July 23, 2007

Research

keywords

  • Axonal Transport
  • Axons
  • RNA-Binding Proteins
  • SUMO-1 Protein

Identity

PubMed Central ID

  • PMC1937566

Scopus Document Identifier

  • 34547857774

Digital Object Identifier (DOI)

  • 10.1073/pnas.0611562104

PubMed ID

  • 17646655

Additional Document Info

volume

  • 104

issue

  • 31