The SRC family protein tyrosine kinase p62(yes) controls polymeric IgA transcytosis in vivo

Frédéric Luton; Marcel Vergés; Jean Pierre Vaerman; Marius Sudol; Keith E. Mostov

doi:10.1016/S1097-2765(00)80213-0

The SRC family protein tyrosine kinase p62(yes) controls polymeric IgA transcytosis in vivo

Frédéric Luton
, Marcel Vergés
, Jean Pierre Vaerman
, Marius Sudol
, Keith E. Mostov

Research output: Contribution to journal › Article › peer-review

82 Scopus citations

Abstract

Transcytosis of polymeric immunoglobulin A (pIgA) across epithelial cells is mediated by the polymeric immunoglobulin receptor (pIgR). Binding of pIgA to pIgR stimulates transcytosis of the pIgA-pIgR complex via a signal transduction pathway that is dependent on a protein tyrosine kinase (PTK) of the SRC family. Here we identify the PTK as p62(yes). We demonstrate the specific physical and functional association of the pIgR with p62(yes) in rodent liver. Analysis of p62(yes) knockout mice revealed a dramatic reduction in the association of tyrosine kinase activity with the pIgR and in transcytosis of pIgA. We conclude that p62(yes) controls pIgA transcytosis in vivo.

Original language	English
Pages (from-to)	627-632
Number of pages	6
Journal	Molecular Cell
Volume	4
Issue number	4
DOIs	https://doi.org/10.1016/S1097-2765(00)80213-0
State	Published - Oct 1999

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@article{9b9e74f43cf442d8b55de15ce4a19826,

title = "The SRC family protein tyrosine kinase p62(yes) controls polymeric IgA transcytosis in vivo",

abstract = "Transcytosis of polymeric immunoglobulin A (pIgA) across epithelial cells is mediated by the polymeric immunoglobulin receptor (pIgR). Binding of pIgA to pIgR stimulates transcytosis of the pIgA-pIgR complex via a signal transduction pathway that is dependent on a protein tyrosine kinase (PTK) of the SRC family. Here we identify the PTK as p62(yes). We demonstrate the specific physical and functional association of the pIgR with p62(yes) in rodent liver. Analysis of p62(yes) knockout mice revealed a dramatic reduction in the association of tyrosine kinase activity with the pIgR and in transcytosis of pIgA. We conclude that p62(yes) controls pIgA transcytosis in vivo.",

author = "Fr{\'e}d{\'e}ric Luton and Marcel Verg{\'e}s and Vaerman, \{Jean Pierre\} and Marius Sudol and Mostov, \{Keith E.\}",

note = "Funding Information: We thank Drs. Brugge, Kraehenbuhl, Morgan, Trowbridge, and Underdown for antibodies. We thank Drs. C. Lowell, P. Soriano, and A. Wilde for helpful discussions; A. Weiss and F. Brodsky for careful reading of the manuscript; and Jeanette Wong for assistance with the manuscript. This work was supported by NIH grant R01AI36953 to K. E. M., NIH grants CA45757 and CA01605 to M. S., ARC grant 94/99-172 from the Direction G{\'e}n{\'e}rale de la Recherche Scientifique-Communaut{\'e} Fran{\c c}aise de Belgique to J.-P. V. M. V. received a fellowship from the Ministerio de Educaci{\'o}n y Cultura, Spain.",

year = "1999",

month = oct,

doi = "10.1016/S1097-2765(00)80213-0",

language = "English",

volume = "4",

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T1 - The SRC family protein tyrosine kinase p62(yes) controls polymeric IgA transcytosis in vivo

AU - Luton, Frédéric

AU - Vergés, Marcel

AU - Vaerman, Jean Pierre

AU - Sudol, Marius

AU - Mostov, Keith E.

N1 - Funding Information: We thank Drs. Brugge, Kraehenbuhl, Morgan, Trowbridge, and Underdown for antibodies. We thank Drs. C. Lowell, P. Soriano, and A. Wilde for helpful discussions; A. Weiss and F. Brodsky for careful reading of the manuscript; and Jeanette Wong for assistance with the manuscript. This work was supported by NIH grant R01AI36953 to K. E. M., NIH grants CA45757 and CA01605 to M. S., ARC grant 94/99-172 from the Direction Générale de la Recherche Scientifique-Communauté Française de Belgique to J.-P. V. M. V. received a fellowship from the Ministerio de Educación y Cultura, Spain.

PY - 1999/10

Y1 - 1999/10

N2 - Transcytosis of polymeric immunoglobulin A (pIgA) across epithelial cells is mediated by the polymeric immunoglobulin receptor (pIgR). Binding of pIgA to pIgR stimulates transcytosis of the pIgA-pIgR complex via a signal transduction pathway that is dependent on a protein tyrosine kinase (PTK) of the SRC family. Here we identify the PTK as p62(yes). We demonstrate the specific physical and functional association of the pIgR with p62(yes) in rodent liver. Analysis of p62(yes) knockout mice revealed a dramatic reduction in the association of tyrosine kinase activity with the pIgR and in transcytosis of pIgA. We conclude that p62(yes) controls pIgA transcytosis in vivo.

AB - Transcytosis of polymeric immunoglobulin A (pIgA) across epithelial cells is mediated by the polymeric immunoglobulin receptor (pIgR). Binding of pIgA to pIgR stimulates transcytosis of the pIgA-pIgR complex via a signal transduction pathway that is dependent on a protein tyrosine kinase (PTK) of the SRC family. Here we identify the PTK as p62(yes). We demonstrate the specific physical and functional association of the pIgR with p62(yes) in rodent liver. Analysis of p62(yes) knockout mice revealed a dramatic reduction in the association of tyrosine kinase activity with the pIgR and in transcytosis of pIgA. We conclude that p62(yes) controls pIgA transcytosis in vivo.

UR - https://www.scopus.com/pages/publications/0033213258

U2 - 10.1016/S1097-2765(00)80213-0

DO - 10.1016/S1097-2765(00)80213-0

M3 - Article

C2 - 10549294

AN - SCOPUS:0033213258

SN - 1097-2765

VL - 4

SP - 627

EP - 632

JO - Molecular Cell

JF - Molecular Cell

IS - 4

ER -

The SRC family protein tyrosine kinase p62(yes) controls polymeric IgA transcytosis in vivo

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