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Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation.

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Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation. / Yeh, Tsung-Yin J; Meyer, Tobias; Meyer-Schwesinger, Catherine; Tsun, Zhi-Yang; Lee, Ray M; Chi, Nai-Wen.

In: BIOCHEM J, Vol. 399, No. 3, 3, 01.11.2006, p. 415-425.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Yeh, T-YJ, Meyer, T, Meyer-Schwesinger, C, Tsun, Z-Y, Lee, RM & Chi, N-W 2006, 'Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation.', BIOCHEM J, vol. 399, no. 3, 3, pp. 415-425. https://doi.org/10.1042/BJ20060713

APA

Yeh, T-Y. J., Meyer, T., Meyer-Schwesinger, C., Tsun, Z-Y., Lee, R. M., & Chi, N-W. (2006). Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation. BIOCHEM J, 399(3), 415-425. [3]. https://doi.org/10.1042/BJ20060713

Vancouver

Yeh T-YJ, Meyer T, Meyer-Schwesinger C, Tsun Z-Y, Lee RM, Chi N-W. Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation. BIOCHEM J. 2006 Nov 1;399(3):415-425. 3. https://doi.org/10.1042/BJ20060713

Bibtex

@article{1895e9c362c640eeb289cd81b9b0d4b6,
title = "Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation.",
abstract = "PARsylation [poly(ADP-ribosyl)ation] of proteins is implicated in the regulation of diverse physiological processes. Tankyrase is a molecular scaffold with this catalytic activity and has been proposed as a regulator of vesicular trafficking on the basis, in part, of its Golgi localization in non-polarized cells. Little is known about tankyrase localization in polarized epithelial cells. Using MDCK (Madin-Darby canine kidney) cells as a model, we found that E-cadherin-mediated intercellular adhesion recruits tankyrase from the cytoplasm to the lateral membrane (including the tight junction), where it stably associates with detergent-insoluble structures. This recruitment is mostly completed within 8 h of calcium-induced formation of cell-cell contact. Conversely, when intercellular adhesion is disrupted by calcium deprivation, tankyrase returns from the lateral membrane to the cytoplasm and becomes more soluble in detergents. The PARsylating activity of tankyrase promotes its dissociation from the lateral membrane as well as its ubiquitination and proteasome-mediated degradation, resulting in an apparent protein half-life of approximately 2 h. Inhibition of tankyrase autoPARsylation using H2O2-induced NAD+ depletion or PJ34 [N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloride] treatment results in tankyrase stabilization and accumulation at the lateral membrane. By contrast, stabilization through proteasome inhibition results in tankyrase accumulation in the cytoplasm. These data suggest that cell-cell contact promotes tankyrase association with the lateral membrane, whereas PARsylating activity promotes translocation to the cytosol, which is followed by ubiquitination and proteasome-mediated degradation. Since the lateral membrane is a sorting station that ensures domain-specific delivery of basolateral membrane proteins, the regulated tankyrase recruitment to this site is consistent with a role in polarized protein targeting in epithelial cells.",
keywords = "Adherens Junctions, Animals, Cadherins, Calcium Chloride, Cell Adhesion, Cell Line, Cell Membrane, Cell Polarity, Cytosol, Detergents, Dogs, Epithelial Cells, Humans, Kidney, Microscopy, Fluorescence, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases, Proteasome Endopeptidase Complex, Protein Processing, Post-Translational, Protein Transport, Recombinant Fusion Proteins, Solubility, Tankyrases, Tight Junctions, Triiodobenzoic Acids, Ubiquitin",
author = "Yeh, {Tsung-Yin J} and Tobias Meyer and Catherine Meyer-Schwesinger and Zhi-Yang Tsun and Lee, {Ray M} and Nai-Wen Chi",
year = "2006",
month = nov,
day = "1",
doi = "10.1042/BJ20060713",
language = "English",
volume = "399",
pages = "415--425",
journal = "BIOCHEM J",
issn = "0264-6021",
publisher = "PORTLAND PRESS LTD",
number = "3",

}

RIS

TY - JOUR

T1 - Tankyrase recruitment to the lateral membrane in polarized epithelial cells: regulation by cell-cell contact and protein poly(ADP-ribosyl)ation.

AU - Yeh, Tsung-Yin J

AU - Meyer, Tobias

AU - Meyer-Schwesinger, Catherine

AU - Tsun, Zhi-Yang

AU - Lee, Ray M

AU - Chi, Nai-Wen

PY - 2006/11/1

Y1 - 2006/11/1

N2 - PARsylation [poly(ADP-ribosyl)ation] of proteins is implicated in the regulation of diverse physiological processes. Tankyrase is a molecular scaffold with this catalytic activity and has been proposed as a regulator of vesicular trafficking on the basis, in part, of its Golgi localization in non-polarized cells. Little is known about tankyrase localization in polarized epithelial cells. Using MDCK (Madin-Darby canine kidney) cells as a model, we found that E-cadherin-mediated intercellular adhesion recruits tankyrase from the cytoplasm to the lateral membrane (including the tight junction), where it stably associates with detergent-insoluble structures. This recruitment is mostly completed within 8 h of calcium-induced formation of cell-cell contact. Conversely, when intercellular adhesion is disrupted by calcium deprivation, tankyrase returns from the lateral membrane to the cytoplasm and becomes more soluble in detergents. The PARsylating activity of tankyrase promotes its dissociation from the lateral membrane as well as its ubiquitination and proteasome-mediated degradation, resulting in an apparent protein half-life of approximately 2 h. Inhibition of tankyrase autoPARsylation using H2O2-induced NAD+ depletion or PJ34 [N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloride] treatment results in tankyrase stabilization and accumulation at the lateral membrane. By contrast, stabilization through proteasome inhibition results in tankyrase accumulation in the cytoplasm. These data suggest that cell-cell contact promotes tankyrase association with the lateral membrane, whereas PARsylating activity promotes translocation to the cytosol, which is followed by ubiquitination and proteasome-mediated degradation. Since the lateral membrane is a sorting station that ensures domain-specific delivery of basolateral membrane proteins, the regulated tankyrase recruitment to this site is consistent with a role in polarized protein targeting in epithelial cells.

AB - PARsylation [poly(ADP-ribosyl)ation] of proteins is implicated in the regulation of diverse physiological processes. Tankyrase is a molecular scaffold with this catalytic activity and has been proposed as a regulator of vesicular trafficking on the basis, in part, of its Golgi localization in non-polarized cells. Little is known about tankyrase localization in polarized epithelial cells. Using MDCK (Madin-Darby canine kidney) cells as a model, we found that E-cadherin-mediated intercellular adhesion recruits tankyrase from the cytoplasm to the lateral membrane (including the tight junction), where it stably associates with detergent-insoluble structures. This recruitment is mostly completed within 8 h of calcium-induced formation of cell-cell contact. Conversely, when intercellular adhesion is disrupted by calcium deprivation, tankyrase returns from the lateral membrane to the cytoplasm and becomes more soluble in detergents. The PARsylating activity of tankyrase promotes its dissociation from the lateral membrane as well as its ubiquitination and proteasome-mediated degradation, resulting in an apparent protein half-life of approximately 2 h. Inhibition of tankyrase autoPARsylation using H2O2-induced NAD+ depletion or PJ34 [N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloride] treatment results in tankyrase stabilization and accumulation at the lateral membrane. By contrast, stabilization through proteasome inhibition results in tankyrase accumulation in the cytoplasm. These data suggest that cell-cell contact promotes tankyrase association with the lateral membrane, whereas PARsylating activity promotes translocation to the cytosol, which is followed by ubiquitination and proteasome-mediated degradation. Since the lateral membrane is a sorting station that ensures domain-specific delivery of basolateral membrane proteins, the regulated tankyrase recruitment to this site is consistent with a role in polarized protein targeting in epithelial cells.

KW - Adherens Junctions

KW - Animals

KW - Cadherins

KW - Calcium Chloride

KW - Cell Adhesion

KW - Cell Line

KW - Cell Membrane

KW - Cell Polarity

KW - Cytosol

KW - Detergents

KW - Dogs

KW - Epithelial Cells

KW - Humans

KW - Kidney

KW - Microscopy, Fluorescence

KW - Poly Adenosine Diphosphate Ribose

KW - Poly(ADP-ribose) Polymerases

KW - Proteasome Endopeptidase Complex

KW - Protein Processing, Post-Translational

KW - Protein Transport

KW - Recombinant Fusion Proteins

KW - Solubility

KW - Tankyrases

KW - Tight Junctions

KW - Triiodobenzoic Acids

KW - Ubiquitin

U2 - 10.1042/BJ20060713

DO - 10.1042/BJ20060713

M3 - SCORING: Journal article

C2 - 16884355

VL - 399

SP - 415

EP - 425

JO - BIOCHEM J

JF - BIOCHEM J

SN - 0264-6021

IS - 3

M1 - 3

ER -