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Structural features and oligomeric nature of human podocin domain

Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and T...

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Autores principales: Mulukala, Sandeep K.N., Irukuvajjula, Shivkumar S., Kumar, Krishan, Garai, Kanchan, Venkatesu, Pannuru, Vadrevu, Ramakrishna, Pasupulati, Anil K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7322680/
https://www.ncbi.nlm.nih.gov/pubmed/32617419
http://dx.doi.org/10.1016/j.bbrep.2020.100774
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author Mulukala, Sandeep K.N.
Irukuvajjula, Shivkumar S.
Kumar, Krishan
Garai, Kanchan
Venkatesu, Pannuru
Vadrevu, Ramakrishna
Pasupulati, Anil K.
author_facet Mulukala, Sandeep K.N.
Irukuvajjula, Shivkumar S.
Kumar, Krishan
Garai, Kanchan
Venkatesu, Pannuru
Vadrevu, Ramakrishna
Pasupulati, Anil K.
author_sort Mulukala, Sandeep K.N.
collection PubMed
description Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and constitute the slit-diaphragm. Podocin is an integral membrane protein attached to the inner membrane of the podocyte via a short transmembrane region (101–125). The cytosolic N- and C-terminus help podocin to attain a hook-like structure. Podocin shares 44% homology with stomatin family proteins and similar to the stomatin proteins, podocin was shown to associate into higher-order oligomers at the site of slit-diaphragm. However, the stoichiometry of the homo-oligomers and how it partakes in the macromolecular assemblies with other slit-diaphragm proteins remains elusive. Here we investigated the oligomeric propensity of a truncated podocin construct (residues:126–350). We show that the podocin domain majorly homo-oligomerizes into a 16-mer. Circular dichroism and fluorescence spectroscopy suggest that the 16-mer oligomer has considerable secondary structure and moderate tertiary packing.
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spelling pubmed-73226802020-07-01 Structural features and oligomeric nature of human podocin domain Mulukala, Sandeep K.N. Irukuvajjula, Shivkumar S. Kumar, Krishan Garai, Kanchan Venkatesu, Pannuru Vadrevu, Ramakrishna Pasupulati, Anil K. Biochem Biophys Rep Research Article Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and constitute the slit-diaphragm. Podocin is an integral membrane protein attached to the inner membrane of the podocyte via a short transmembrane region (101–125). The cytosolic N- and C-terminus help podocin to attain a hook-like structure. Podocin shares 44% homology with stomatin family proteins and similar to the stomatin proteins, podocin was shown to associate into higher-order oligomers at the site of slit-diaphragm. However, the stoichiometry of the homo-oligomers and how it partakes in the macromolecular assemblies with other slit-diaphragm proteins remains elusive. Here we investigated the oligomeric propensity of a truncated podocin construct (residues:126–350). We show that the podocin domain majorly homo-oligomerizes into a 16-mer. Circular dichroism and fluorescence spectroscopy suggest that the 16-mer oligomer has considerable secondary structure and moderate tertiary packing. Elsevier 2020-06-25 /pmc/articles/PMC7322680/ /pubmed/32617419 http://dx.doi.org/10.1016/j.bbrep.2020.100774 Text en © 2020 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Mulukala, Sandeep K.N.
Irukuvajjula, Shivkumar S.
Kumar, Krishan
Garai, Kanchan
Venkatesu, Pannuru
Vadrevu, Ramakrishna
Pasupulati, Anil K.
Structural features and oligomeric nature of human podocin domain
title Structural features and oligomeric nature of human podocin domain
title_full Structural features and oligomeric nature of human podocin domain
title_fullStr Structural features and oligomeric nature of human podocin domain
title_full_unstemmed Structural features and oligomeric nature of human podocin domain
title_short Structural features and oligomeric nature of human podocin domain
title_sort structural features and oligomeric nature of human podocin domain
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7322680/
https://www.ncbi.nlm.nih.gov/pubmed/32617419
http://dx.doi.org/10.1016/j.bbrep.2020.100774
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