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Plekhh2, a novel po...
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Perisic, LjubicaKarolinska Institutet
(author)
Plekhh2, a novel podocyte protein downregulated in human focal segmental glomerulosclerosis, is involved in matrix adhesion and actin dynamics
- Article/chapterEnglish2012
Publisher, publication year, extent ...
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Elsevier BV,2012
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:kth-107084
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https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-107084URI
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https://doi.org/10.1038/ki.2012.252DOI
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http://kipublications.ki.se/Default.aspx?queryparsed=id:125568957URI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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QC 20121210
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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.
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Added entries (persons, corporate bodies, meetings, titles ...)
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Lal, Mark
(author)
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Hulkko, Jenny
(author)
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Hultenby, KjellKarolinska Institutet
(author)
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Önfelt, BjörnKarolinska Institutet,KTH,Cellens fysik(Swepub:kth)u1tquq43
(author)
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Sun, Ying
(author)
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Dunér, FredrikKarolinska Institutet
(author)
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Patrakka, JaakkoKarolinska Institutet
(author)
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Betsholtz, ChristerKarolinska Institutet
(author)
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Uhlén, MathiasKTH,Proteomik(Swepub:kth)u1dulvmw
(author)
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Brismar, HjalmarKarolinska Institutet,KTH,Cellens fysik(Swepub:kth)u1232ew5
(author)
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Tryggvason, KarlKarolinska Institutet
(author)
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Wernerson, AnnikaKarolinska Institutet
(author)
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Pikkarainen, Timo
(author)
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Karolinska InstitutetCellens fysik
(creator_code:org_t)
Related titles
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In:Kidney International: Elsevier BV82:10, s. 1071-10830085-25381523-1755
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Perisic, Ljubica
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Lal, Mark
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Hulkko, Jenny
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Hultenby, Kjell
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Önfelt, Björn
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Sun, Ying
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Dunér, Fredrik
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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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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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Kidney Internati ...
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Royal Institute of Technology
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Karolinska Institutet