Rab14 regulates apical targeting in polarized epithelial cells

Khameeka N. Kitt, Delia Hernández-Deviez, Sarah D. Ballantyne, Elias T. Spiliotis, James E. Casanova, Jean Wilson

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.

Original languageEnglish (US)
Pages (from-to)1218-1231
Number of pages14
JournalTraffic
Volume9
Issue number7
DOIs
StatePublished - Jul 2008

Fingerprint

trans-Golgi Network
Machinery
Membrane Proteins
Epithelial Cells
Membranes
Guanosine
Endosomes
Vasoactive Intestinal Peptide
Glutathione Transferase
Sorting
Yeast
Recycling
Proteins
Tissue
Epithelium
Yeasts
Maintenance

Keywords

  • Apical targeting
  • Epithelial cells
  • Polarity
  • Rab14

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Structural Biology
  • Molecular Biology
  • Genetics

Cite this

Kitt, K. N., Hernández-Deviez, D., Ballantyne, S. D., Spiliotis, E. T., Casanova, J. E., & Wilson, J. (2008). Rab14 regulates apical targeting in polarized epithelial cells. Traffic, 9(7), 1218-1231. https://doi.org/10.1111/j.1600-0854.2008.00752.x

Rab14 regulates apical targeting in polarized epithelial cells. / Kitt, Khameeka N.; Hernández-Deviez, Delia; Ballantyne, Sarah D.; Spiliotis, Elias T.; Casanova, James E.; Wilson, Jean.

In: Traffic, Vol. 9, No. 7, 07.2008, p. 1218-1231.

Research output: Contribution to journalArticle

Kitt, KN, Hernández-Deviez, D, Ballantyne, SD, Spiliotis, ET, Casanova, JE & Wilson, J 2008, 'Rab14 regulates apical targeting in polarized epithelial cells', Traffic, vol. 9, no. 7, pp. 1218-1231. https://doi.org/10.1111/j.1600-0854.2008.00752.x
Kitt KN, Hernández-Deviez D, Ballantyne SD, Spiliotis ET, Casanova JE, Wilson J. Rab14 regulates apical targeting in polarized epithelial cells. Traffic. 2008 Jul;9(7):1218-1231. https://doi.org/10.1111/j.1600-0854.2008.00752.x
Kitt, Khameeka N. ; Hernández-Deviez, Delia ; Ballantyne, Sarah D. ; Spiliotis, Elias T. ; Casanova, James E. ; Wilson, Jean. / Rab14 regulates apical targeting in polarized epithelial cells. In: Traffic. 2008 ; Vol. 9, No. 7. pp. 1218-1231.
@article{06a38fbeeecc47499ec2fc9e989fee9d,
title = "Rab14 regulates apical targeting in polarized epithelial cells",
abstract = "Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.",
keywords = "Apical targeting, Epithelial cells, Polarity, Rab14",
author = "Kitt, {Khameeka N.} and Delia Hern{\'a}ndez-Deviez and Ballantyne, {Sarah D.} and Spiliotis, {Elias T.} and Casanova, {James E.} and Jean Wilson",
year = "2008",
month = "7",
doi = "10.1111/j.1600-0854.2008.00752.x",
language = "English (US)",
volume = "9",
pages = "1218--1231",
journal = "Traffic",
issn = "1398-9219",
publisher = "Blackwell Munksgaard",
number = "7",

}

TY - JOUR

T1 - Rab14 regulates apical targeting in polarized epithelial cells

AU - Kitt, Khameeka N.

AU - Hernández-Deviez, Delia

AU - Ballantyne, Sarah D.

AU - Spiliotis, Elias T.

AU - Casanova, James E.

AU - Wilson, Jean

PY - 2008/7

Y1 - 2008/7

N2 - Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.

AB - Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.

KW - Apical targeting

KW - Epithelial cells

KW - Polarity

KW - Rab14

UR - http://www.scopus.com/inward/record.url?scp=46349088941&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=46349088941&partnerID=8YFLogxK

U2 - 10.1111/j.1600-0854.2008.00752.x

DO - 10.1111/j.1600-0854.2008.00752.x

M3 - Article

C2 - 18429929

AN - SCOPUS:46349088941

VL - 9

SP - 1218

EP - 1231

JO - Traffic

JF - Traffic

SN - 1398-9219

IS - 7

ER -