βA3/A1-crystallin regulates apical polarity and EGFR endocytosis in retinal pigmented epithelial cells.

Animals Cell Polarity / genetics Cytoskeletal Proteins / metabolism Endocytosis Epithelial Cells / metabolism ErbB Receptors / metabolism Humans Mice, Knockout Phosphatidylinositol 4,5-Diphosphate / metabolism Phospholipid Transfer Proteins / metabolism Phosphorylation Protein Binding Retinal Pigment Epithelium / cytology beta-Crystallin A Chain / genetics

Journal

Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179

Informations de publication

Date de publication:
08 07 2021
Historique:
received: 19 06 2020
accepted: 24 06 2021
entrez: 9 7 2021
pubmed: 10 7 2021
medline: 17 8 2021
Statut: epublish

Résumé

The retinal pigmented epithelium (RPE) is a monolayer of multifunctional cells located at the back of the eye. High membrane turnover and polarization, including formation of actin-based apical microvilli, are essential for RPE function and retinal health. Herein, we demonstrate an important role for βA3/A1-crystallin in RPE. βA3/A1-crystallin deficiency leads to clathrin-mediated epidermal growth factor receptor (EGFR) endocytosis abnormalities and actin network disruption at the apical side that result in RPE polarity disruption and degeneration. We found that βA3/A1-crystallin binds to phosphatidylinositol transfer protein (PITPβ) and that βA3/A1-crystallin deficiency diminishes phosphatidylinositol 4,5-biphosphate (PI(4,5)P

Identifiants

DOI: 10.1038/s42003-021-02386-6 PMID: 34239035 PMC: PMC8266859
pubmed: 34239035
doi: 10.1038/s42003-021-02386-6
pii: 10.1038/s42003-021-02386-6
pmc: PMC8266859
doi:

Substances chimiques

Cryba1 protein, mouse 0
Cytoskeletal Proteins 0
Phosphatidylinositol 4,5-Diphosphate 0
Phospholipid Transfer Proteins 0
beta-Crystallin A Chain 0
ezrin 0
ErbB Receptors EC 2.7.10.1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

850

Subventions

Organisme : NEI NIH HHS
ID : R01 EY000871
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY019037
Pays : United States

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Auteurs

Peng Shang (P)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Nadezda Stepicheva (N)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Kenneth Teel (K)

Dean McGee Eye Institute, University of Oklahoma Health Science Center, Oklahoma City, OK, USA.

Austin McCauley (A)

Dean McGee Eye Institute, University of Oklahoma Health Science Center, Oklahoma City, OK, USA.

Christopher Scott Fitting (CS)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Stacey Hose (S)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Rhonda Grebe (R)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Meysam Yazdankhah (M)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Sayan Ghosh (S)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Haitao Liu (H)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Anastasia Strizhakova (A)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
ORCID: 0000-0002-3476-3888

Joseph Weiss (J)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Imran A Bhutto (IA)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Gerard A Lutty (GA)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Ashwath Jayagopal (A)

Kodiak Sciences, Palo Alto, CA, USA.

Jiang Qian (J)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
ORCID: 0000-0002-0476-3596

José-Alain Sahel (JA)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Institut de la Vision, INSERM, CNRS, Sorbonne Université, Paris, France.
ORCID: 0000-0002-4831-1153

J Samuel Zigler (J)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

James T Handa (JT)

Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Yuri Sergeev (Y)

National Eye Institute, National Institutes of Health, Bethesda, MD, USA.
ORCID: 0000-0002-7204-6572

Raju V S Rajala (RVS)

Dean McGee Eye Institute, University of Oklahoma Health Science Center, Oklahoma City, OK, USA.

Simon Watkins (S)

Department of Cell Biology and Center for Biologic Imaging, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
ORCID: 0000-0003-4092-1552

Debasish Sinha (D)

Department of Ophthalmology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. Debasish@pitt.edu.
Wilmer Eye Institute, The Johns Hopkins University School of Medicine, Baltimore, MD, USA. Debasish@pitt.edu.
Department of Cell Biology and Center for Biologic Imaging, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. Debasish@pitt.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Polarité de la cellule › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Endocytose › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Cellules › Cellules épithéliales › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur facteur croissance › Récepteurs ErbB › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souris transgéniques › Souris knockout › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Lipides › Lipides membranaires › Phospholipides › Glycérophosphate › Acides phosphatidiques › Glycérophospholipides › Phosphatidyl inositols › Phosphates phosphatidylinositol › Phosphatidylinositol diphosphate-4,5 › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transfert des phospholipides › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Métabolisme › Phosphorylation › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Organes des sens › Oeil › Rétine › Épithélium pigmentaire de la rétine › βA3/A1-crystallin regulates apical polarity...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de l'oeil › Cristallines › Cristallines-bêta › Chaîne A de la cristalline-bêta › βA3/A1-crystallin regulates apical polarity...