Unable to connect to database - 08:21:58 Unable to connect to database - 08:21:58 SQL Statement is null or not a SELECT - 08:21:58 SQL Statement is null or not a DELETE - 08:21:58 Botany & Plant Biology 2007 - Abstract Search
Unable to connect to database - 08:21:58 Unable to connect to database - 08:21:58 SQL Statement is null or not a SELECT - 08:21:58

Abstract Detail

Protein Targeting and Vesicular Trafficking

Kim, Sang-Jin [1], Bassham, Diane [2].

A putative Golgin in Arabidopsis vacuolar trafficking.

Vacuoles in plants have many functions, such as maintaining turgor within the cell, compartmentalizing toxic materials, recycling degraded proteins and holding storage proteins. Essential vacuolar proteins are transported via the vacuolar trafficking system that consists of endoplasmic reticulum (ER), Golgi apparatus (GA), Trans-golgi network (TGN), and pre-vacuolar compartment (PVC). At1g24460 (p200) is a component of VPS45 complex which is associated with vacuolar trafficking in the TGN. p200 was identified by co-immunoprecipitation with SYP41, which is another component in the VPS45 complex. p200 has a C-terminal transmembrane domain was found to be localized to the GA by Immunofluorescence with golgi marker protein, sialyl transferase. Treatment with the GA disruption agent, Bredfeldin A (BFA), revealed that while other golgi proteins were shifted back to the ER, p200 still remained in the cytoplasm. This is a strong feature of mammalian golgin, and p200 has a similar structure. From the results of BFA treatment, p200 seems to function by maintaining GA structure in Arabidopsis. To study its specific function, a homozygous p200 T-DNA knock-out mutant was identified. The knock-out mutant showed increased sensitivity to both NaCl and mannitol-induced osmotic stress. p200 knock-out mutant also exhibited decreased root growth under KCl and LiCl stresses. To characterize the differences between ionic and non-ionic osmotic sensitive phenotype, 2D gel analysis of vacuolar proteins in p200 knock mutant is being pursued. In conclusion, as a component of the AtVPS45 complex, p200 is a putative golgin in vacuolar trafficking and important in maintaining golgi structure according to our findings.

Log in to add this item to your schedule

1 - Iowa State University, GDCB, 434 Bessey Hall, Iowa State University, Ames, Iowa, 50010, USA
2 - Iowa State University, GDCB


Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P22032
Abstract ID:1842

Copyright 2000-2007, Botanical Society of America. All rights