Search: id:"swepub:oai:DiVA.org:kth-107084" >
Plekhh2, a novel po...
Plekhh2, a novel podocyte protein downregulated in human focal segmental glomerulosclerosis, is involved in matrix adhesion and actin dynamics
-
- Perisic, Ljubica (author)
- Karolinska Institutet
-
Lal, Mark (author)
-
Hulkko, Jenny (author)
-
show more...
-
- Hultenby, Kjell (author)
- Karolinska Institutet
-
- Önfelt, Björn (author)
- Karolinska Institutet,KTH,Cellens fysik
-
Sun, Ying (author)
-
- Dunér, Fredrik (author)
- Karolinska Institutet
-
- Patrakka, Jaakko (author)
- Karolinska Institutet
-
- Betsholtz, Christer (author)
- Karolinska Institutet
-
- Uhlén, Mathias (author)
- KTH,Proteomik
-
- Brismar, Hjalmar (author)
- Karolinska Institutet,KTH,Cellens fysik
-
- Tryggvason, Karl (author)
- Karolinska Institutet
-
- Wernerson, Annika (author)
- Karolinska Institutet
-
Pikkarainen, Timo (author)
-
show less...
-
(creator_code:org_t)
- Elsevier BV, 2012
- 2012
- English.
-
In: Kidney International. - : Elsevier BV. - 0085-2538 .- 1523-1755. ; 82:10, s. 1071-1083
- Related links:
-
http://www.kidney-in...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
http://kipublication...
-
show less...
Abstract
Subject headings
Close
- Pleckstrin homology domain-containing, family H (with MyTH4 domain), member 2 (Plekhh2) is a 1491-residue intracellular protein highly enriched in renal glomerular podocytes for which no function has been ascribed. Analysis of renal biopsies from patients with focal segmental glomerulosclerosis revealed a significant reduction in total podocyte Plekhh2 expression compared to controls. Sequence analysis indicated a putative a-helical coiled-coil segment as the only recognizable domain within the N-terminal half of the polypeptide, while the C-terminal half contains two PH, a MyTH4, and a FERM domain. We identified a phosphatidylinositol-3-phosphate consensus-binding site in the PH1 domain required for Plekhh2 localization to peripheral regions of cell lamellipodia. The N-terminal half of Plekkh2 is not necessary for lamellipodial targeting but mediates self-association. Yeast two-hybrid screening showed that Plekhh2 directly interacts through its FERM domain with the focal adhesion protein Hic-5 and actin. Plekhh2 and Hic-5 coprecipitated and colocalized at the soles of podocyte foot processes in situ and Hic-5 partially relocated from focal adhesions to lamellipodia in Plekhh2-expressing podocytes. In addition, Plekhh2 stabilizes the cortical actin cytoskeleton by attenuating actin depolymerization. Our findings suggest a structural and functional role for Plekhh2 in the podocyte foot processes.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- cell biology and structure
- cell-matrix interactions
- cytoskeleton
- podocyte
- protein interaction
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Perisic, Ljubica
-
Lal, Mark
-
Hulkko, Jenny
-
Hultenby, Kjell
-
Önfelt, Björn
-
Sun, Ying
-
show more...
-
Dunér, Fredrik
-
Patrakka, Jaakko
-
Betsholtz, Chris ...
-
Uhlén, Mathias
-
Brismar, Hjalmar
-
Tryggvason, Karl
-
Wernerson, Annik ...
-
Pikkarainen, Tim ...
-
show less...
- About the subject
-
- NATURAL SCIENCES
-
NATURAL SCIENCES
-
and Biological Scien ...
- Articles in the publication
-
Kidney Internati ...
- By the university
-
Royal Institute of Technology
-
Karolinska Institutet