JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M400544200 on April 28, 2004

J. Biol. Chem., Vol. 279, Issue 28, 29728-29739, July 9, 2004
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
279/28/29728    most recent
M400544200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rundle, D. R.
Right arrow Articles by Tsiokas, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rundle, D. R.
Right arrow Articles by Tsiokas, L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

PKD2 Interacts and Co-localizes with mDia1 to Mitotic Spindles of Dividing Cells

ROLE OF mDia1 IN PKD2 LOCALIZATION TO MITOTIC SPINDLES*

Dana R. Rundle{ddagger}, Gary Gorbsky{ddagger}§, and Leonidas Tsiokas{ddagger}

From the {ddagger}Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104 and the §Molecular, Cell, and Developmental Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104

Mutations in pkd2 result in the type 2 form of autosomal dominant polycystic kidney disease, which accounts for ~15% of all cases of the disease. PKD2, the protein product of pkd2, belongs to the transient receptor potential superfamily of cation channels, and it can function as a mechanosensitive channel in the primary cilium of kidney cells, an intracellular Ca2+ release channel in the endoplasmic reticulum, and/or a nonselective cation channel in the plasma membrane. We have identified mDia1/Drf1 (mammalian Diaphanous or Diaphanous-related formin 1 protein) as a PKD2-interacting protein by yeast two-hybrid screen. mDia1 is a member of the RhoA GTPase-binding formin homology protein family that participates in cytoskeletal organization, cytokinesis, and signal transduction. We show that mDia1 and PKD2 interact in native and in transfected cells, and binding is mediated by the cytoplasmic C terminus of PKD2 binding to the mDia1 N terminus. The interaction is more prevalent in dividing cells in which endogenous PKD2 and mDia1 co-localize to the mitotic spindles. RNA interference experiments reveal that endogenous mDia1 knockdown in HeLa cells results in the loss of PKD2 from mitotic spindles and alters intracellular Ca2+ release. Our results suggest that mDia1 facilitates the movement of PKD2 to a centralized position during cell division and has a positive effect on intracellular Ca2+ release during mitosis. This may be important to ensure equal segregation of PKD2 to the daughter cell to maintain a necessary level of channel activity. Alternatively, PKD2 channel activity may be important in the cell division process or in cell fate decisions after division.

Received for publication, January 17, 2004 , and in revised form, April 13, 2004.

* This work is supported by a postdoctoral fellowship from the Polycystic Kidney Disease Foundation (to D. R. R.) and National Institutes of Health Grant DK59599 (to L. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 405-271-8001 (ext. 46211); Fax: 405-271-3758; E-mail: leonidas-tsiokas{at}ouhsc.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Cardiovasc ResHome page
C. S. Nicolas, K.-H. Park, A. El Harchi, J. Camonis, R. S. Kass, D. Escande, J. Merot, G. Loussouarn, F. Le Bouffant, and I. Baro
IKs response to protein kinase A-dependent KCNQ1 phosphorylation requires direct interaction with microtubules
Cardiovasc Res, August 1, 2008; 79(3): 427 - 435.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
F. Bartolini, J. B. Moseley, J. Schmoranzer, L. Cassimeris, B. L. Goode, and G. G. Gundersen
The formin mDia2 stabilizes microtubules independently of its actin nucleation activity
J. Cell Biol., May 1, 2008; 181(3): 523 - 536.
[Abstract] [Full Text] [PDF]

Home page
 J. Med. Genet.Home page
M Adams, U M Smith, C V Logan, and C A Johnson
Recent advances in the molecular pathology, cell biology and genetics of ciliopathies
J. Med. Genet., May 1, 2008; 45(5): 257 - 267.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
J. Du, M. Ding, S. Sours-Brothers, S. Graham, and R. Ma
Mediation of angiotensin II-induced Ca2+ signaling by polycystin 2 in glomerular mesangial cells
Am J Physiol Renal Physiol, April 1, 2008; 294(4): F909 - F918.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
S. Fan, V. Fogg, Q. Wang, X.-W. Chen, C.-J. Liu, and B. Margolis
A novel Crumbs3 isoform regulates cell division and ciliogenesis via importin {beta} interactions
J. Cell Biol., July 24, 2007; 178(3): 387 - 398.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
T. Benzing, M. Simons, and G. Walz
Wnt Signaling in Polycystic Kidney Disease
J. Am. Soc. Nephrol., May 1, 2007; 18(5): 1389 - 1398.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
N. Montalbetti, Q. Li, Y. Wu, X.-Z. Chen, and H. F. Cantiello
Polycystin-2 cation channel function in the human syncytiotrophoblast is regulated by microtubular structures
J. Physiol., March 15, 2007; 579(3): 717 - 728.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Q. Li, N. Montalbetti, Y. Wu, A. Ramos, M. K. Raychowdhury, X.-Z. Chen, and H. F. Cantiello
Polycystin-2 Cation Channel Function Is under the Control of Microtubular Structures in Primary Cilia of Renal Epithelial Cells
J. Biol. Chem., December 8, 2006; 281(49): 37566 - 37575.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
Y. Wu, X.-Q. Dai, Q. Li, C. X. Chen, W. Mai, Z. Hussain, W. Long, N. Montalbetti, G. Li, R. Glynne, et al.
Kinesin-2 mediates physical and functional interactions between polycystin-2 and fibrocystin
Hum. Mol. Genet., November 15, 2006; 15(22): 3280 - 3292.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
A. R. Gallagher, S. Hoffmann, N. Brown, A. Cedzich, S. Meruvu, D. Podlich, Y. Feng, V. Konecke, U. de Vries, H.-P. Hammes, et al.
A Truncated Polycystin-2 Protein Causes Polycystic Kidney Disease and Retinal Degeneration in Transgenic Rats
J. Am. Soc. Nephrol., October 1, 2006; 17(10): 2719 - 2730.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
T. Obara, S. Mangos, Y. Liu, J. Zhao, S. Wiessner, A. G. Kramer-Zucker, F. Olale, A. F. Schier, and I. A. Drummond
Polycystin-2 Immunolocalization and Function in Zebrafish
J. Am. Soc. Nephrol., October 1, 2006; 17(10): 2706 - 2718.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
E.-F. Bui-Xuan, Q. Li, X.-Z. Chen, C. A. Boucher, R. Sandford, J. Zhou, and N. Basora
More than colocalizing with polycystin-1, polycystin-L is in the centrosome
Am J Physiol Renal Physiol, August 1, 2006; 291(2): F395 - F406.
[Abstract] [Full Text] [PDF]

Home page
 DevelopmentHome page
H. Shiratori and H. Hamada
The left-right axis in the mouse: from origin to morphology
Development, June 1, 2006; 133(11): 2095 - 2104.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
L. Geng, D. Okuhara, Z. Yu, X. Tian, Y. Cai, S. Shibazaki, and S. Somlo
Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif
J. Cell Sci., April 1, 2006; 119(7): 1383 - 1395.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
R. Ma, W.-P. Li, D. Rundle, J. Kong, H. I. Akbarali, and L. Tsiokas
PKD2 Functions as an Epidermal Growth Factor-Activated Plasma Membrane Channel
Mol. Cell. Biol., September 15, 2005; 25(18): 8285 - 8298.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
Q. Li, N. Montalbetti, P. Y. Shen, X.-Q. Dai, C. I. Cheeseman, E. Karpinski, G. Wu, H. F. Cantiello, and X.-Z. Chen
Alpha-actinin associates with polycystin-2 and regulates its channel activity
Hum. Mol. Genet., June 15, 2005; 14(12): 1587 - 1603.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Puri, B. S. Magenheimer, R. L. Maser, E. M. Ryan, C. A. Zien, D. D. Walker, D. P. Wallace, S. J. Hempson, and J. P. Calvet
Polycystin-1 Activates the Calcineurin/NFAT (Nuclear Factor of Activated T-cells) Signaling Pathway
J. Biol. Chem., December 31, 2004; 279(53): 55455 - 55464.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.