| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 49, 46544-46552, December 7, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Renal Unit, Massachusetts General Hospital and Harvard
Medical School, Charlestown, Massachusetts 02129
Polycystin-1, the protein defective in a majority
of patients with autosomal dominant polycystic kidney disease, is a
ubiquitously expressed multi-span transmembrane protein of unknown
function. Subcellular localization studies found this protein to be a
component of various cell junctional complexes and to be associated
with the cytoskeleton, but the specificity and nature of such
associations are not known. To identify proteins that interact with the
polycystin-1 C-tail (P1CT), this segment was used as bait in a yeast
two-hybrid screening of a kidney epithelial cell library. The
intermediate filament (IF) protein vimentin was identified as a strong
polycystin-1-interacting partner. Cytokeratins K8 and K18 and desmin
were also found to interact with P1CT. These interactions were mediated
by coiled-coil motifs in polycystin-1 and IF proteins. Vimentin,
cytokeratins K8 and K18, and desmin also bound directly to P1CT in GST
pull-down and in in vitro filament assembly assays. Two
observations confirmed these interactions in vivo: (i) a
cell membrane-anchored form of recombinant P1CT decorated the IF
network and was found to associate with the cytoskeleton in
detergent-solubilized cells and (ii) endogenous polycystin-1
distributed with IF at desmosomal junctions. Polycystin-1 may utilize
this association for structural, storage, or signaling functions.
Polycystin-1 Interacts with Intermediate
Filaments*
,
*
This work is supported by National Institutes of Health
Grant P01 DK54711.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a National Institutes of Health training grant.
§
Supported by a National Kidney Foundation research fellowship.
¶
To whom correspondence should be addressed: Renal Unit,
Massachusetts General Hospital, Bldg. 149, 13th St., Charlestown, MA
02129. Tel.: 617-726-5663; Fax: 617-726-5671; E-mail:
arnaout@receptor.mgh.harvard.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  T. Weimbs Polycystic kidney disease and renal injury repair: common pathways, fluid flow, and the function of polycystin-1 Am J Physiol Renal Physiol, November 1, 2007; 293(5): F1423 - F1432. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Joly, S. Ishibe, C. Nickel, Z. Yu, S. Somlo, and L. G. Cantley The Polycystin 1-C-terminal Fragment Stimulates ERK-dependent Spreading of Renal Epithelial Cells J. Biol. Chem., September 8, 2006; 281(36): 26329 - 26339. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
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]
|
|
|
|
|
|
F. Qian, W. Wei, G. Germino, and A. Oberhauser The Nanomechanics of Polycystin-1 Extracellular Region J. Biol. Chem., December 9, 2005; 280(49): 40723 - 40730. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Valkova, R. Yunis, S. K. Mak, K. Kang, and D. Kultz Nek8 Mutation Causes Overexpression of Galectin-1, Sorcin, and Vimentin and Accumulation of the Major Urinary Protein in Renal Cysts of jck Mice Mol. Cell. Proteomics, July 1, 2005; 4(7): 1009 - 1018. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 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]
|
|
|
|
|
|
V. Babich, W.-Z. Zeng, B.-I. Yeh, O. Ibraghimov-Beskrovnaya, Y. Cai, S. Somlo, and C.-L. Huang The N-terminal Extracellular Domain Is Required for Polycystin-1-dependent Channel Activity J. Biol. Chem., June 11, 2004; 279(24): 25582 - 25589. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. F. Cantiello Regulation of calcium signaling by polycystin-2 Am J Physiol Renal Physiol, June 1, 2004; 286(6): F1012 - F1029. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. H. Grimm, Y. Cai, V. Chauvet, V. Rajendran, R. Zeltner, L. Geng, E. D. Avner, W. Sweeney, S. Somlo, and M. J. Caplan Polycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells J. Biol. Chem., September 19, 2003; 278(38): 36786 - 36793. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. J. Streets, L. J. Newby, M. J. O'Hare, N. O. Bukanov, O. Ibraghimov-Beskrovnaya, and A. C.M. Ong Functional Analysis of PKD1 Transgenic Lines Reveals a Direct Role for Polycystin-1 in Mediating Cell-Cell Adhesion J. Am. Soc. Nephrol., July 1, 2003; 14(7): 1804 - 1815. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. M. Xu, S. Gonzalez-Perrett, M. Essafi, G. A. Timpanaro, N. Montalbetti, M. A. Arnaout, and H. F. Cantiello Polycystin-1 Activates and Stabilizes the Polycystin-2 Channel J. Biol. Chem., January 10, 2003; 278(3): 1457 - 1462. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Igarashi and S. Somlo Genetics and Pathogenesis of Polycystic Kidney Disease J. Am. Soc. Nephrol., September 1, 2002; 13(9): 2384 - 2398. [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 |
