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Plekhh2, a novel po...
Plekhh2, a novel podocyte protein downregulated in human focal segmental glomerulosclerosis, is involved in matrix adhesion and actin dynamics
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- Perisic, Ljubica (författare)
- Karolinska Institutet
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Lal, Mark (författare)
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Hulkko, Jenny (författare)
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- Hultenby, Kjell (författare)
- Karolinska Institutet
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- Önfelt, Björn (författare)
- Karolinska Institutet,KTH,Cellens fysik
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Sun, Ying (författare)
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- Dunér, Fredrik (författare)
- Karolinska Institutet
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- Patrakka, Jaakko (författare)
- Karolinska Institutet
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- Betsholtz, Christer (författare)
- Karolinska Institutet
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- Uhlén, Mathias (författare)
- KTH,Proteomik
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- Brismar, Hjalmar (författare)
- Karolinska Institutet,KTH,Cellens fysik
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- Tryggvason, Karl (författare)
- Karolinska Institutet
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- Wernerson, Annika (författare)
- Karolinska Institutet
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Pikkarainen, Timo (författare)
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(creator_code:org_t)
- Elsevier BV, 2012
- 2012
- Engelska.
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Ingår i: Kidney International. - : Elsevier BV. - 0085-2538 .- 1523-1755. ; 82:10, s. 1071-1083
- Relaterad länk:
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http://www.kidney-in...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- cell biology and structure
- cell-matrix interactions
- cytoskeleton
- podocyte
- protein interaction
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas
- Av författaren/redakt...
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Perisic, Ljubica
-
Lal, Mark
-
Hulkko, Jenny
-
Hultenby, Kjell
-
Önfelt, Björn
-
Sun, Ying
-
visa fler...
-
Dunér, Fredrik
-
Patrakka, Jaakko
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Betsholtz, Chris ...
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Uhlén, Mathias
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Brismar, Hjalmar
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Tryggvason, Karl
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Wernerson, Annik ...
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Pikkarainen, Tim ...
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visa färre...
- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
- Artiklar i publikationen
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Kidney Internati ...
- Av lärosätet
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Kungliga Tekniska Högskolan
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Karolinska Institutet