Skip to main content
padlock icon - secure page this page is secure

Free Content Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors

Download Article:
 Download
(PDF 568.5 kb)
 
Summary

We have studied the transport of proricin and pro2S albumin to the protein storage vacuoles of developing castor bean (Ricinus communis L.) endosperm. Immunoelectron microscopy and cell fractionation reveal that both proteins travel through the Golgi apparatus and co-localize throughout their route to the storage vacuole. En route to the PSV, the proteins co-localize in large (>200 nm) vesicles, which are likely to represent developing storage vacuoles. We further show that the sequence-specific vacuolar sorting signals of both proricin and pro2SA bind in vitro to proteins that have high sequence similarity to members of the VSR/AtELP/BP-80 vacuolar sorting receptor family, generally associated with clathrin-mediated traffic to the lytic vacuole. The implications of these findings in relation to the current model for protein sorting to storage vacuoles are discussed.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: albumin; ricin; sorting receptor; storage proteins; vacuole

Document Type: Research Article

Affiliations: 1: Research School of Biological and Molecular Sciences, Oxford Brookes University, Gipsy Lane Campus, Oxford OX3 0BP, UK 2: Mass Spectrometry Unit, DIBIT-HSR, via Olgettina 58, 20132 Milan, Italy 3: Istituto di Biologia e Biotecnologia Agraria, CNR, via Bassini 15, 20133 Milan, Italy

Publication date: September 1, 2004

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more