Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3

Joseph T. Roland, Anne K. Kenworthy, Johan Peranen, Steven H Caplan, James R. Goldenring

Research output: Contribution to journalArticle

111 Citations (Scopus)

Abstract

Cells use multiple pathways to internalize and recycle cell surface components. Although Rab11a and Myosin Vb are involved in the recycling of proteins internalized by clathrin-mediated endocytosis, Rab8a has been implicated in nonclathrin-dependent endocytosis and recycling. By yeast two-hybrid assays, we have now demonstrated that Myosin Vb can interact with Rab8a, but not Rab8b. We have confirmed the interaction of Myosin Vb with Rab11a and Rab8a in vivo by using fluorescent resonant energy transfer techniques. Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. Myosin Vb tail can cause the accumulation of both Rab11a and Rab8a in collapsed membrane cisternae, whereas dominant-negative Rab11-FIP2(129-512) selectively accumulates Rab11a but not Rab8a. Additionally, dynamic live cell imaging demonstrates distinct pathways for Rab11a and Rab8a vesicle trafficking. These findings indicate that Rab8a and Rab11a define different recycling pathways that both use Myosin Vb.

Original languageEnglish (US)
Pages (from-to)2828-2837
Number of pages10
JournalMolecular biology of the cell
Volume18
Issue number8
DOIs
StatePublished - Aug 1 2007

Fingerprint

Myosins
Recycling
Endocytosis
Clathrin
Two-Hybrid System Techniques
Energy Transfer
Cellular Structures
Membranes
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. / Roland, Joseph T.; Kenworthy, Anne K.; Peranen, Johan; Caplan, Steven H; Goldenring, James R.

In: Molecular biology of the cell, Vol. 18, No. 8, 01.08.2007, p. 2828-2837.

Research output: Contribution to journalArticle

Roland, Joseph T. ; Kenworthy, Anne K. ; Peranen, Johan ; Caplan, Steven H ; Goldenring, James R. / Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. In: Molecular biology of the cell. 2007 ; Vol. 18, No. 8. pp. 2828-2837.
@article{64c816f8b1ee4b54b5e8be2be4882a07,
title = "Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3",
abstract = "Cells use multiple pathways to internalize and recycle cell surface components. Although Rab11a and Myosin Vb are involved in the recycling of proteins internalized by clathrin-mediated endocytosis, Rab8a has been implicated in nonclathrin-dependent endocytosis and recycling. By yeast two-hybrid assays, we have now demonstrated that Myosin Vb can interact with Rab8a, but not Rab8b. We have confirmed the interaction of Myosin Vb with Rab11a and Rab8a in vivo by using fluorescent resonant energy transfer techniques. Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. Myosin Vb tail can cause the accumulation of both Rab11a and Rab8a in collapsed membrane cisternae, whereas dominant-negative Rab11-FIP2(129-512) selectively accumulates Rab11a but not Rab8a. Additionally, dynamic live cell imaging demonstrates distinct pathways for Rab11a and Rab8a vesicle trafficking. These findings indicate that Rab8a and Rab11a define different recycling pathways that both use Myosin Vb.",
author = "Roland, {Joseph T.} and Kenworthy, {Anne K.} and Johan Peranen and Caplan, {Steven H} and Goldenring, {James R.}",
year = "2007",
month = "8",
day = "1",
doi = "10.1091/mbc.E07-02-0169",
language = "English (US)",
volume = "18",
pages = "2828--2837",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "8",

}

TY - JOUR

T1 - Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3

AU - Roland, Joseph T.

AU - Kenworthy, Anne K.

AU - Peranen, Johan

AU - Caplan, Steven H

AU - Goldenring, James R.

PY - 2007/8/1

Y1 - 2007/8/1

N2 - Cells use multiple pathways to internalize and recycle cell surface components. Although Rab11a and Myosin Vb are involved in the recycling of proteins internalized by clathrin-mediated endocytosis, Rab8a has been implicated in nonclathrin-dependent endocytosis and recycling. By yeast two-hybrid assays, we have now demonstrated that Myosin Vb can interact with Rab8a, but not Rab8b. We have confirmed the interaction of Myosin Vb with Rab11a and Rab8a in vivo by using fluorescent resonant energy transfer techniques. Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. Myosin Vb tail can cause the accumulation of both Rab11a and Rab8a in collapsed membrane cisternae, whereas dominant-negative Rab11-FIP2(129-512) selectively accumulates Rab11a but not Rab8a. Additionally, dynamic live cell imaging demonstrates distinct pathways for Rab11a and Rab8a vesicle trafficking. These findings indicate that Rab8a and Rab11a define different recycling pathways that both use Myosin Vb.

AB - Cells use multiple pathways to internalize and recycle cell surface components. Although Rab11a and Myosin Vb are involved in the recycling of proteins internalized by clathrin-mediated endocytosis, Rab8a has been implicated in nonclathrin-dependent endocytosis and recycling. By yeast two-hybrid assays, we have now demonstrated that Myosin Vb can interact with Rab8a, but not Rab8b. We have confirmed the interaction of Myosin Vb with Rab11a and Rab8a in vivo by using fluorescent resonant energy transfer techniques. Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. Myosin Vb tail can cause the accumulation of both Rab11a and Rab8a in collapsed membrane cisternae, whereas dominant-negative Rab11-FIP2(129-512) selectively accumulates Rab11a but not Rab8a. Additionally, dynamic live cell imaging demonstrates distinct pathways for Rab11a and Rab8a vesicle trafficking. These findings indicate that Rab8a and Rab11a define different recycling pathways that both use Myosin Vb.

UR - http://www.scopus.com/inward/record.url?scp=34547810829&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34547810829&partnerID=8YFLogxK

U2 - 10.1091/mbc.E07-02-0169

DO - 10.1091/mbc.E07-02-0169

M3 - Article

VL - 18

SP - 2828

EP - 2837

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 8

ER -