Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING CELLS 1 – a glycosyltransferase (GT64) related to the animal exostosins
Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING CELLS 1 – a glycosyltransferase (GT64) related to the animal exostosins
Despite the fact that several hundred glycosyltransferases have been identified from sequencing of plant genomes, the biological functions of only a handful have been established to date. A Poplar glycosyltransferase 64 (GT64) family member that is differentially expressed during the cell division and elongation phases of cambial growth was identified from previously generated transcript profiling of cambium tissues. The predicted Poplar GT64 protein has a closely related Arabidopsis homolog ECTOPICALLY PARTING CELLS (EPC1). Mutation of the EPC1 gene, one of three Arabidopsis GT64 family members, results in plants with a dramatically reduced growth habit, defects in vascular formation and reduced cell–cell adhesion properties in hypocotyl and cotyledon tissues. Secondary growth is enhanced in epc1 hypocotyl tissues and it is proposed that this results from the abnormal cell–cell adhesion within the cortical parenchyma cell layers. Loss of cell–cell contacts within cotyledon and leaf tissues is also proposed to account for vascular patterning defects and the fragile nature of epc1 tissues. The EPC1 protein thus plays a critical role during plant development in maintaining the integrity of organs via cell–cell adhesion, thereby providing mechanical strength and facilitating the movement of metabolites throughout the plant.
glycosyltransferasecell adhesionArabidopsiscell walls
384-397
Singh, Sunil Kumar
d71334ea-c957-4fbd-9e10-60a2a30ee446
Eland, Cathlene
9b35c49f-e227-4267-9013-bacc829eb340
Harholt, Jesper
36ca7bf2-8930-46cf-a3dc-0a57767f6d52
Scheller, Henrik Vibe
a751b13f-62f4-4f71-b815-006079cacee0
Marchant, Alan
3e54d51c-53b0-4df0-b428-2e73b071ee8e
2005
Singh, Sunil Kumar
d71334ea-c957-4fbd-9e10-60a2a30ee446
Eland, Cathlene
9b35c49f-e227-4267-9013-bacc829eb340
Harholt, Jesper
36ca7bf2-8930-46cf-a3dc-0a57767f6d52
Scheller, Henrik Vibe
a751b13f-62f4-4f71-b815-006079cacee0
Marchant, Alan
3e54d51c-53b0-4df0-b428-2e73b071ee8e
Singh, Sunil Kumar, Eland, Cathlene, Harholt, Jesper, Scheller, Henrik Vibe and Marchant, Alan
(2005)
Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING CELLS 1 – a glycosyltransferase (GT64) related to the animal exostosins.
The Plant Journal, 43 (3), .
(doi:10.1111/j.1365-313X.2005.02455.x).
Abstract
Despite the fact that several hundred glycosyltransferases have been identified from sequencing of plant genomes, the biological functions of only a handful have been established to date. A Poplar glycosyltransferase 64 (GT64) family member that is differentially expressed during the cell division and elongation phases of cambial growth was identified from previously generated transcript profiling of cambium tissues. The predicted Poplar GT64 protein has a closely related Arabidopsis homolog ECTOPICALLY PARTING CELLS (EPC1). Mutation of the EPC1 gene, one of three Arabidopsis GT64 family members, results in plants with a dramatically reduced growth habit, defects in vascular formation and reduced cell–cell adhesion properties in hypocotyl and cotyledon tissues. Secondary growth is enhanced in epc1 hypocotyl tissues and it is proposed that this results from the abnormal cell–cell adhesion within the cortical parenchyma cell layers. Loss of cell–cell contacts within cotyledon and leaf tissues is also proposed to account for vascular patterning defects and the fragile nature of epc1 tissues. The EPC1 protein thus plays a critical role during plant development in maintaining the integrity of organs via cell–cell adhesion, thereby providing mechanical strength and facilitating the movement of metabolites throughout the plant.
This record has no associated files available for download.
More information
Published date: 2005
Keywords:
glycosyltransferasecell adhesionArabidopsiscell walls
Identifiers
Local EPrints ID: 45412
URI: http://eprints.soton.ac.uk/id/eprint/45412
ISSN: 0960-7412
PURE UUID: 5f43f86f-c200-4e26-8984-b429e5161080
Catalogue record
Date deposited: 29 Mar 2007
Last modified: 15 Mar 2024 09:10
Export record
Altmetrics
Contributors
Author:
Sunil Kumar Singh
Author:
Cathlene Eland
Author:
Jesper Harholt
Author:
Henrik Vibe Scheller
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics