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ABCB19/PGP19 stabilises PIN1 in membrane microdomains in Arabidopsis

Boosaree Titapiwatanakun, Joshua Blakeslee, Anindita Bandyopadhyay, Haibing Yang, Jozef Mravec UGent, Michael Sauer, Yan Cheng, Jiri Adamec, Akitomo Nagashima and Markus Geisler, et al. (2009) Plant Journal. 57(1). p.27-44
abstract
Auxin transport is mediated at the cellular level by three independent mechanisms that are characterised by the PIN-formed (PIN), P-glycoprotein (ABCB/PGP) and AUX/LAX transport proteins. The PIN and ABCB transport proteins, best represented by PIN1 and ABCB19 (PGP19), have been shown to coordinately regulate auxin efflux. When PIN1 and ABCB19 coincide on the plasma membrane, their interaction enhances the rate and specificity of auxin efflux and the dynamic cycling of PIN1 is reduced. However, ABCB19 function is not regulated by the dynamic cellular trafficking mechanisms that regulate PIN1 in apical tissues, as localisation of ABCB19 on the plasma membrane was not inhibited by short-term treatments with latrunculin B, oryzalin, brefeldin A (BFA) or wortmannin - all of which have been shown to alter PIN1 and/or PIN2 plasma membrane localisation. When taken up by endocytosis, the styryl dye FM4-64 labels diffuse rather than punctuate intracellular bodies in abcb19 (pgp19), and some aggregations of PIN1 induced by short-term BFA treatment did not disperse after BFA washout in abcb19. Although the subcellular localisations of ABCB19 and PIN1 in the reciprocal mutant backgrounds were like those in wild type, PIN1 plasma membrane localisation in abcb19 roots was more easily perturbed by the detergent Triton X-100, but not other non-ionic detergents. ABCB19 is stably associated with sterol/sphingolipid-enriched membrane fractions containing BIG/TIR3 and partitions into Triton X-100 detergent-resistant membrane (DRM) fractions. In the wild type, PIN1 was also present in DRMs, but was less abundant in abcb19 DRMs. These observations suggested a rationale for the observed lack of auxin transport activity when PIN1 is expressed in a non-plant heterologous system. PIN1 was therefore expressed in Schizosaccharomyces pombe, which has plant-like sterol-enriched microdomains, and catalysed auxin transport in these cells. These data suggest that ABCB19 stabilises PIN1 localisation at the plasma membrane in discrete cellular subdomains where PIN1 and ABCB19 expression overlaps.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
lipid raft, auxin transport, detergent-resistant membrane, P-glycoprotein, PIN1, multi-drug resistance protein, trafficking
journal title
Plant Journal
Plant J.
volume
57
issue
1
pages
27 - 44
Web of Science type
Review
Web of Science id
000261962700003
JCR category
PLANT SCIENCES
JCR impact factor
6.946 (2009)
JCR rank
6/172 (2009)
JCR quartile
1 (2009)
ISSN
0960-7412
DOI
10.1111/j.1365-313X.2008.03668.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I don't know the status of the copyright for this publication
id
528370
handle
http://hdl.handle.net/1854/LU-528370
date created
2009-03-23 15:55:04
date last changed
2009-04-01 16:28:43
@article{528370,
  abstract     = {Auxin transport is mediated at the cellular level by three independent mechanisms that are characterised by the PIN-formed (PIN), P-glycoprotein (ABCB/PGP) and AUX/LAX transport proteins. The PIN and ABCB transport proteins, best represented by PIN1 and ABCB19 (PGP19), have been shown to coordinately regulate auxin efflux. When PIN1 and ABCB19 coincide on the plasma membrane, their interaction enhances the rate and specificity of auxin efflux and the dynamic cycling of PIN1 is reduced. However, ABCB19 function is not regulated by the dynamic cellular trafficking mechanisms that regulate PIN1 in apical tissues, as localisation of ABCB19 on the plasma membrane was not inhibited by short-term treatments with latrunculin B, oryzalin, brefeldin A (BFA) or wortmannin - all of which have been shown to alter PIN1 and/or PIN2 plasma membrane localisation. When taken up by endocytosis, the styryl dye FM4-64 labels diffuse rather than punctuate intracellular bodies in abcb19 (pgp19), and some aggregations of PIN1 induced by short-term BFA treatment did not disperse after BFA washout in abcb19. Although the subcellular localisations of ABCB19 and PIN1 in the reciprocal mutant backgrounds were like those in wild type, PIN1 plasma membrane localisation in abcb19 roots was more easily perturbed by the detergent Triton X-100, but not other non-ionic detergents. ABCB19 is stably associated with sterol/sphingolipid-enriched membrane fractions containing BIG/TIR3 and partitions into Triton X-100 detergent-resistant membrane (DRM) fractions. In the wild type, PIN1 was also present in DRMs, but was less abundant in abcb19 DRMs. These observations suggested a rationale for the observed lack of auxin transport activity when PIN1 is expressed in a non-plant heterologous system. PIN1 was therefore expressed in Schizosaccharomyces pombe, which has plant-like sterol-enriched microdomains, and catalysed auxin transport in these cells. These data suggest that ABCB19 stabilises PIN1 localisation at the plasma membrane in discrete cellular subdomains where PIN1 and ABCB19 expression overlaps.},
  author       = {Titapiwatanakun, Boosaree and Blakeslee, Joshua and Bandyopadhyay, Anindita and Yang, Haibing and Mravec, Jozef and Sauer, Michael and Cheng, Yan and Adamec, Jiri and Nagashima, Akitomo and Geisler, Markus and Sakai, Tatsuya and Friml, Jiri and Peer, Wendy Ann and Murphy, Angus},
  issn         = {0960-7412},
  journal      = {Plant Journal},
  keyword      = {lipid raft,auxin transport,detergent-resistant membrane,P-glycoprotein,PIN1,multi-drug resistance protein,trafficking},
  language     = {eng},
  number       = {1},
  pages        = {27--44},
  title        = {ABCB19/PGP19 stabilises PIN1 in membrane microdomains in Arabidopsis},
  url          = {http://dx.doi.org/10.1111/j.1365-313X.2008.03668.x},
  volume       = {57},
  year         = {2009},
}

Chicago
Titapiwatanakun, Boosaree, Joshua Blakeslee, Anindita Bandyopadhyay, Haibing Yang, Jozef Mravec, Michael Sauer, Yan Cheng, et al. 2009. “ABCB19/PGP19 Stabilises PIN1 in Membrane Microdomains in Arabidopsis.” Plant Journal 57 (1): 27–44.
APA
Titapiwatanakun, B., Blakeslee, J., Bandyopadhyay, A., Yang, H., Mravec, J., Sauer, M., Cheng, Y., et al. (2009). ABCB19/PGP19 stabilises PIN1 in membrane microdomains in Arabidopsis. Plant Journal, 57(1), 27–44.
Vancouver
1.
Titapiwatanakun B, Blakeslee J, Bandyopadhyay A, Yang H, Mravec J, Sauer M, et al. ABCB19/PGP19 stabilises PIN1 in membrane microdomains in Arabidopsis. Plant Journal. 2009;57(1):27–44.
MLA
Titapiwatanakun, Boosaree, Joshua Blakeslee, Anindita Bandyopadhyay, et al. “ABCB19/PGP19 Stabilises PIN1 in Membrane Microdomains in Arabidopsis.” Plant Journal 57.1 (2009): 27–44. Print.