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A plant-specific subclass of C-terminal kinesins contains a conserved A-type cyclin-dependent kinase site implicated in folding and dimerization

Vanstraelen, Marleen UGent, Torres Acosta, Juan Antonio, De Veylder, Lieven UGent, Inzé, Dirk UGent and Geelen, Danny UGent (2004) PLANT PHYSIOLOGY. 135(3). p.1417-1429
abstract
Cyclin-dependent kinases (CDKs) control cell cycle progression through timely coordinated phosphorylation events. Two kmesin-like proteins that interact with CDKA;1 were identified and designated KCA1 and KCA2. They are 81% identical and have a similar three-partite domain organization. The N-terminal domain contains an ATP and microtubule-binding site typical for kinesin motors. A green fluorescent protein (GFP) fusion of the N-terminal domain of KCA1 decorated microtubules in Bright Yellow-2 cells, demonstrating microtubule-binding activity. During cytokinesis the full-length GFP-fusion protein accumulated at the midline of young and mature expanding phragmoplasts. Two-hybrid analysis and coimmunoprecipitation experiments showed that coiled-coil structures of the central stalk were responsible for homo- and heterodimerization of KCA1 and KCA2. By western-blot analysis, high molecular mass KCA molecules were detected in extracts from Bright Yellow-2 cells overproducing the full-length GFP fusion. Treatment of these cultures with the phosphatase inhibitor vanadate caused an accumulation of these KCA molecules. In addition to dimerization, interactions within the C-terminally located tail domain were revealed, indicating that the tail could fold onto itself. The tail domains of KCA1 and KCA2 contained two adjacent putative CDKA;1 phosphorylation sites, one of which is conserved in KCA homologs from other plant species. Site-directed mutagenesis of the conserved phosphorylation sites in KCA1 resulted in a reduced binding with CDKA;1 and abolished intramolecular tail interactions. The data show that phosphorylation of the CDKA;1 site provokes a conformational change in the structure of KCA with implications in folding and dimerization.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
CELL-CYCLE, CALMODULIN-BINDING PROTEIN, MICROTUBULE DYNAMICS, SPINDLE FORMATION, IN-VIVO, ARABIDOPSIS, MOTOR, PHOSPHORYLATION, CYTOSKELETON, CYTOKINESIS
journal title
PLANT PHYSIOLOGY
Plant Physiol.
volume
135
issue
3
pages
1417 - 1429
Web of Science type
Article
Web of Science id
000222692700025
JCR category
PLANT SCIENCES
JCR impact factor
5.881 (2004)
JCR rank
7/137 (2004)
JCR quartile
1 (2004)
ISSN
0032-0889
DOI
10.1104/pp.104.044818
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
299671
handle
http://hdl.handle.net/1854/LU-299671
date created
2005-03-09 17:42:00
date last changed
2016-12-19 15:43:23
@article{299671,
  abstract     = {Cyclin-dependent kinases (CDKs) control cell cycle progression through timely coordinated phosphorylation events. Two kmesin-like proteins that interact with CDKA;1 were identified and designated KCA1 and KCA2. They are 81\% identical and have a similar three-partite domain organization. The N-terminal domain contains an ATP and microtubule-binding site typical for kinesin motors. A green fluorescent protein (GFP) fusion of the N-terminal domain of KCA1 decorated microtubules in Bright Yellow-2 cells, demonstrating microtubule-binding activity. During cytokinesis the full-length GFP-fusion protein accumulated at the midline of young and mature expanding phragmoplasts. Two-hybrid analysis and coimmunoprecipitation experiments showed that coiled-coil structures of the central stalk were responsible for homo- and heterodimerization of KCA1 and KCA2. By western-blot analysis, high molecular mass KCA molecules were detected in extracts from Bright Yellow-2 cells overproducing the full-length GFP fusion. Treatment of these cultures with the phosphatase inhibitor vanadate caused an accumulation of these KCA molecules. In addition to dimerization, interactions within the C-terminally located tail domain were revealed, indicating that the tail could fold onto itself. The tail domains of KCA1 and KCA2 contained two adjacent putative CDKA;1 phosphorylation sites, one of which is conserved in KCA homologs from other plant species. Site-directed mutagenesis of the conserved phosphorylation sites in KCA1 resulted in a reduced binding with CDKA;1 and abolished intramolecular tail interactions. The data show that phosphorylation of the CDKA;1 site provokes a conformational change in the structure of KCA with implications in folding and dimerization.},
  author       = {Vanstraelen, Marleen and Torres Acosta, Juan Antonio and De Veylder, Lieven and Inz{\'e}, Dirk and Geelen, Danny},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keyword      = {CELL-CYCLE,CALMODULIN-BINDING PROTEIN,MICROTUBULE DYNAMICS,SPINDLE FORMATION,IN-VIVO,ARABIDOPSIS,MOTOR,PHOSPHORYLATION,CYTOSKELETON,CYTOKINESIS},
  language     = {eng},
  number       = {3},
  pages        = {1417--1429},
  title        = {A plant-specific subclass of C-terminal kinesins contains a conserved A-type cyclin-dependent kinase site implicated in folding and dimerization},
  url          = {http://dx.doi.org/10.1104/pp.104.044818},
  volume       = {135},
  year         = {2004},
}

Chicago
Vanstraelen, Marleen, Juan Antonio Torres Acosta, Lieven De Veylder, Dirk Inzé, and Danny Geelen. 2004. “A Plant-specific Subclass of C-terminal Kinesins Contains a Conserved A-type Cyclin-dependent Kinase Site Implicated in Folding and Dimerization.” Plant Physiology 135 (3): 1417–1429.
APA
Vanstraelen, M., Torres Acosta, J. A., De Veylder, L., Inzé, D., & Geelen, D. (2004). A plant-specific subclass of C-terminal kinesins contains a conserved A-type cyclin-dependent kinase site implicated in folding and dimerization. PLANT PHYSIOLOGY, 135(3), 1417–1429.
Vancouver
1.
Vanstraelen M, Torres Acosta JA, De Veylder L, Inzé D, Geelen D. A plant-specific subclass of C-terminal kinesins contains a conserved A-type cyclin-dependent kinase site implicated in folding and dimerization. PLANT PHYSIOLOGY. 2004;135(3):1417–29.
MLA
Vanstraelen, Marleen, Juan Antonio Torres Acosta, Lieven De Veylder, et al. “A Plant-specific Subclass of C-terminal Kinesins Contains a Conserved A-type Cyclin-dependent Kinase Site Implicated in Folding and Dimerization.” PLANT PHYSIOLOGY 135.3 (2004): 1417–1429. Print.