Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles

Neuron. 1998 Jul;21(1):111-22. doi: 10.1016/s0896-6273(00)80519-x.

Abstract

The mouse mutant mocha, a model for the Hermansky-Pudlak storage pool deficiency syndrome, is characterized by defective platelets, coat and eye color dilution, lysosomal abnormalities, inner ear degeneration, and neurological deficits. Here, we show that mocha is a null allele of the delta subunit of the adaptor-like protein complex AP-3, which is associated with coated vesicles budding from the trans-Golgi network, and that AP-3 is missing in mocha tissues. In mocha brain, the ZnT-3 transporter is reduced, resulting in a lack of zinc-associated Timm historeactivity in hippocampal mossy fibers. Our results demonstrate that the AP-3 complex is responsible for cargo selection to lysosome-related organelles such as melanosomes and platelet dense granules as well as to neurotransmitter vesicles.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Protein Complex 3
  • Adaptor Protein Complex beta Subunits
  • Alleles
  • Animals
  • Base Sequence
  • Biological Transport / physiology
  • Blood Platelets / metabolism*
  • Central Nervous System / metabolism
  • Chromosome Mapping
  • Endosomes / metabolism*
  • Gene Rearrangement
  • Melanocytes / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Mutation / genetics*
  • Platelet Storage Pool Deficiency / genetics*
  • Platelet Storage Pool Deficiency / metabolism
  • RNA, Messenger / metabolism
  • Synaptic Vesicles / metabolism*
  • Transcription Factors / genetics*
  • Transcription, Genetic
  • Zinc / metabolism

Substances

  • Adaptor Protein Complex 3
  • Adaptor Protein Complex beta Subunits
  • Ap3d1 protein, mouse
  • RNA, Messenger
  • Transcription Factors
  • Zinc