Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells

Lise Anne Denmat-Ouisse, Céline Phebidias, Päivi Honkavaara, Philippe Robin, Blandine Geny, Do Sik Min, Sylvain Bourgoin, Michael A. Frohman, Marie Noëlle Raymond

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Phospholipase D (PLD) plays a central role in the control of vesicle budding and protein transit. We previously showed that in resting epithelial HT29-cl19A cells, PLD is implicated in the control of constitutive protein transit, from the trans-Golgi network to the plasma membrane, and that phorbol ester stimulation of protein transit is correlated with PLD activation (Auger, R., Robin, P., Camier, B., Vial, G., Rossignol, B., Tenu, J.-P., and Raymond, M.-N. (1999) J. Biol. Chem. 274, 28652-28659). In this paper we demonstrate that: 1) PLD is not implicated in the earliest phases of protein transit; 2) PLD controls apical but not basolateral protein transit; 3) HT29-cl19A cells express PLD1b and PLD2a mRNAs and proteins; 4) the expression of a catalytically inactive mutant of PLD2 (mPLD2-K758R) significantly inhibited apical constitutive protein transit whereas expression of a catalytically inactive mutant of PLD1 (hPLD1b-K898R) prevented increases in the rate of apical transit as triggered by phorbol esters; 5) PLD2 appears to be located in a perinuclear region containing the Golgi whereas PLD1, which is scattered in the cytoplasm in resting cells, is translocated to the plasma membrane after phorbol ester stimulation. Taken together, these data lead to the conclusion that in HT29-cl19A cells, both PLDs regulate protein transit between the trans-Golgi network and the apical plasma membrane, but that they do so at different steps in the pathway.

Original languageEnglish
Pages (from-to)48840-48846
Number of pages7
JournalJournal of Biological Chemistry
Volume276
Issue number52
DOIs
Publication statusPublished - 2001 Dec 28

Fingerprint

Phospholipase D
HT29 Cells
Proteins
Phorbol Esters
Cell membranes
trans-Golgi Network
Cell Membrane
Songbirds
Cytoplasm
Epithelial Cells
Chemical activation
Messenger RNA

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Denmat-Ouisse, L. A., Phebidias, C., Honkavaara, P., Robin, P., Geny, B., Min, D. S., ... Raymond, M. N. (2001). Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells. Journal of Biological Chemistry, 276(52), 48840-48846. https://doi.org/10.1074/jbc.M104276200
Denmat-Ouisse, Lise Anne ; Phebidias, Céline ; Honkavaara, Päivi ; Robin, Philippe ; Geny, Blandine ; Min, Do Sik ; Bourgoin, Sylvain ; Frohman, Michael A. ; Raymond, Marie Noëlle. / Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 52. pp. 48840-48846.
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Denmat-Ouisse, LA, Phebidias, C, Honkavaara, P, Robin, P, Geny, B, Min, DS, Bourgoin, S, Frohman, MA & Raymond, MN 2001, 'Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells', Journal of Biological Chemistry, vol. 276, no. 52, pp. 48840-48846. https://doi.org/10.1074/jbc.M104276200

Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells. / Denmat-Ouisse, Lise Anne; Phebidias, Céline; Honkavaara, Päivi; Robin, Philippe; Geny, Blandine; Min, Do Sik; Bourgoin, Sylvain; Frohman, Michael A.; Raymond, Marie Noëlle.

In: Journal of Biological Chemistry, Vol. 276, No. 52, 28.12.2001, p. 48840-48846.

Research output: Contribution to journalArticle

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T1 - Regulation of Constitutive Protein Transit by Phospholipase D in HT29-cl19A Cells

AU - Denmat-Ouisse, Lise Anne

AU - Phebidias, Céline

AU - Honkavaara, Päivi

AU - Robin, Philippe

AU - Geny, Blandine

AU - Min, Do Sik

AU - Bourgoin, Sylvain

AU - Frohman, Michael A.

AU - Raymond, Marie Noëlle

PY - 2001/12/28

Y1 - 2001/12/28

N2 - Phospholipase D (PLD) plays a central role in the control of vesicle budding and protein transit. We previously showed that in resting epithelial HT29-cl19A cells, PLD is implicated in the control of constitutive protein transit, from the trans-Golgi network to the plasma membrane, and that phorbol ester stimulation of protein transit is correlated with PLD activation (Auger, R., Robin, P., Camier, B., Vial, G., Rossignol, B., Tenu, J.-P., and Raymond, M.-N. (1999) J. Biol. Chem. 274, 28652-28659). In this paper we demonstrate that: 1) PLD is not implicated in the earliest phases of protein transit; 2) PLD controls apical but not basolateral protein transit; 3) HT29-cl19A cells express PLD1b and PLD2a mRNAs and proteins; 4) the expression of a catalytically inactive mutant of PLD2 (mPLD2-K758R) significantly inhibited apical constitutive protein transit whereas expression of a catalytically inactive mutant of PLD1 (hPLD1b-K898R) prevented increases in the rate of apical transit as triggered by phorbol esters; 5) PLD2 appears to be located in a perinuclear region containing the Golgi whereas PLD1, which is scattered in the cytoplasm in resting cells, is translocated to the plasma membrane after phorbol ester stimulation. Taken together, these data lead to the conclusion that in HT29-cl19A cells, both PLDs regulate protein transit between the trans-Golgi network and the apical plasma membrane, but that they do so at different steps in the pathway.

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