Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
. 2005 May;58(1):109-22.
doi: 10.1007/s11103-005-4618-4.

Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein

Luciana Renna  1 , Sally L Hanton, Giovanni Stefano, Lauren Bortolotti, Vikram Misra, Federica Brandizzi
Affiliations
Comparative Study

Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein

Luciana Renna et al. Plant Mol Biol. 2005 May.

Abstract

Golgins are a family of coiled-coil proteins that are associated with the Golgi apparatus. They are necessary for tethering events in membrane fusion and may act as structural support for Golgi cisternae. Here we report on the identification of an Arabidopsis golgin which is a homologue of CASP, a known transmembrane mammalian and yeast golgin. Similar to its homologues, the plant CASP contains a long N-terminal coiled-coil region protruding into the cytosol and a C-terminal transmembrane domain with amino acid residues which are highly conserved across species. Through fluorescent protein tagging experiments, we show that plant CASP localizes at the plant Golgi apparatus and that the C-terminus of this protein is sufficient for its localization, as has been shown for its mammalian counterpart. In addition, we demonstrate that the plant CASP is able to localize at the mammalian Golgi apparatus. However, mutagenesis of a conserved tyrosine in the transmembrane domain revealed that it is necessary for ER export and Golgi localization of the Arabidopsis CASP in mammalian cells, but is not required for its correct localization in plant cells. These data suggest that mammalian and plant cells have different mechanisms for concentrating CASP in the Golgi apparatus.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. J Cell Sci. 2004 Feb 29;117(Pt 6):943-54 - PubMed
    1. Plant Cell. 1999 Nov;11(11):2233-48 - PubMed
    1. Ann Bot. 2003 Aug;92(2):167-80 - PubMed
    1. Curr Biol. 1999 Apr 8;9(7):377-80 - PubMed
    1. J Mol Biol. 2001 Jan 19;305(3):567-80 - PubMed

Publication types

MeSH terms