A study first reported from the Society for Neuroscience annual meeting last November has just been published in the April 19 Journal of Neuroscience. Gunnar Gouras and colleagues at Weill Medical College of Cornell University in New York City describe how intraneuronal amyloid-β interrupts multivesicular body (MVB) sorting by impairing the ubiquitin proteasome system. First author Claudia Almeida and colleagues tracked MVB sorting of epidermal growth factor receptor (EGFR) in neurons from transgenic mice expressing mutant human amyloid-β precursor protein. As Almeida revealed in Washington, intraneuronal Aβ, localized to late endosomes in neurons from these animals, appears to impair EGFR processing in a ubiquitin proteasome system-dependent manner. For full coverage, read our ARF related conference story.—Tom Fagan.

Reference:
Almeida GC, Takahashi RH, Gouras GK. Beta-Amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. The Journal of Neuroscience. April 19, 2006;26:4277-4288. Abstract

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References

News Citations

  1. SfN: Where, How Does Intraneuronal Aβ Pack Its Punch? Part 3

Paper Citations

  1. . Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci. 2006 Apr 19;26(16):4277-88. PubMed.

Further Reading

Papers

  1. . Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci. 2006 Apr 19;26(16):4277-88. PubMed.

Primary Papers

  1. . Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci. 2006 Apr 19;26(16):4277-88. PubMed.