Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain

Brigitte Heller, Emmanuel Adu-Gyamfi, Whitney Smith-Kinnaman, Cliff Babbey, Mohsin Vora, Yi Xue, Robert Bittman, Robert Stahelin, Clark Wells

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Polarity proteins promote the asymmetric organization of cells by orienting intracellular sorting mechanisms, such as protein trafficking and cytoskeletal assembly. The localization of individual polarity proteins in turn is often determined by association with factors that mediate contact with other cells or the substratum. This arrangement for the Par and Crb apical polarity complexes at the tight junction is disrupted by the adaptor protein Amot. Amot directly binds the scaffolding proteins Patj and Mupp1 and redistributes them and their binding partners from the plasma membrane to endosomes. However, the mechanism by which Amot is targeted to endosomes is unknown. Here, a novel lipid binding domain within Amot is shown to selectively bind with high affinity to membranes containing monophosphorylated phosphatidylinositols and cholesterol. With similar lipid specificity, Amot inserts into and tubulates membranes in vitro and enlarges perinuclear endosomal compartments in cells. Based on the similar distribution of Amot with cholesterol, Rab11, and Arf6, such membrane interactions are identified at juxtanuclear endocytic recycling compartments. Taken together, these findings indicate that Amot is targeted along with associated apical polarity proteins to the endocytic recycling compartment via this novel membrane binding domain.

Original languageEnglish
Pages (from-to)12308-12320
Number of pages13
JournalJournal of Biological Chemistry
Volume285
Issue number16
DOIs
StatePublished - Apr 16 2010

Fingerprint

Recycling
Lipids
Membranes
Endosomes
Proteins
Cholesterol
Tight Junctions
Protein Transport
Phosphatidylinositols
Die casting inserts
Cell membranes
Sorting
Cell Membrane

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain. / Heller, Brigitte; Adu-Gyamfi, Emmanuel; Smith-Kinnaman, Whitney; Babbey, Cliff; Vora, Mohsin; Xue, Yi; Bittman, Robert; Stahelin, Robert; Wells, Clark.

In: Journal of Biological Chemistry, Vol. 285, No. 16, 16.04.2010, p. 12308-12320.

Research output: Contribution to journalArticle

Heller, B, Adu-Gyamfi, E, Smith-Kinnaman, W, Babbey, C, Vora, M, Xue, Y, Bittman, R, Stahelin, R & Wells, C 2010, 'Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain', Journal of Biological Chemistry, vol. 285, no. 16, pp. 12308-12320. https://doi.org/10.1074/jbc.M109.096230
Heller B, Adu-Gyamfi E, Smith-Kinnaman W, Babbey C, Vora M, Xue Y et al. Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain. Journal of Biological Chemistry. 2010 Apr 16;285(16):12308-12320. https://doi.org/10.1074/jbc.M109.096230
Heller, Brigitte ; Adu-Gyamfi, Emmanuel ; Smith-Kinnaman, Whitney ; Babbey, Cliff ; Vora, Mohsin ; Xue, Yi ; Bittman, Robert ; Stahelin, Robert ; Wells, Clark. / Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain. In: Journal of Biological Chemistry. 2010 ; Vol. 285, No. 16. pp. 12308-12320.
@article{4c9c0aa8f3884d0daef7755451ca027a,
title = "Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain",
abstract = "Polarity proteins promote the asymmetric organization of cells by orienting intracellular sorting mechanisms, such as protein trafficking and cytoskeletal assembly. The localization of individual polarity proteins in turn is often determined by association with factors that mediate contact with other cells or the substratum. This arrangement for the Par and Crb apical polarity complexes at the tight junction is disrupted by the adaptor protein Amot. Amot directly binds the scaffolding proteins Patj and Mupp1 and redistributes them and their binding partners from the plasma membrane to endosomes. However, the mechanism by which Amot is targeted to endosomes is unknown. Here, a novel lipid binding domain within Amot is shown to selectively bind with high affinity to membranes containing monophosphorylated phosphatidylinositols and cholesterol. With similar lipid specificity, Amot inserts into and tubulates membranes in vitro and enlarges perinuclear endosomal compartments in cells. Based on the similar distribution of Amot with cholesterol, Rab11, and Arf6, such membrane interactions are identified at juxtanuclear endocytic recycling compartments. Taken together, these findings indicate that Amot is targeted along with associated apical polarity proteins to the endocytic recycling compartment via this novel membrane binding domain.",
author = "Brigitte Heller and Emmanuel Adu-Gyamfi and Whitney Smith-Kinnaman and Cliff Babbey and Mohsin Vora and Yi Xue and Robert Bittman and Robert Stahelin and Clark Wells",
year = "2010",
month = "4",
day = "16",
doi = "10.1074/jbc.M109.096230",
language = "English",
volume = "285",
pages = "12308--12320",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain

AU - Heller, Brigitte

AU - Adu-Gyamfi, Emmanuel

AU - Smith-Kinnaman, Whitney

AU - Babbey, Cliff

AU - Vora, Mohsin

AU - Xue, Yi

AU - Bittman, Robert

AU - Stahelin, Robert

AU - Wells, Clark

PY - 2010/4/16

Y1 - 2010/4/16

N2 - Polarity proteins promote the asymmetric organization of cells by orienting intracellular sorting mechanisms, such as protein trafficking and cytoskeletal assembly. The localization of individual polarity proteins in turn is often determined by association with factors that mediate contact with other cells or the substratum. This arrangement for the Par and Crb apical polarity complexes at the tight junction is disrupted by the adaptor protein Amot. Amot directly binds the scaffolding proteins Patj and Mupp1 and redistributes them and their binding partners from the plasma membrane to endosomes. However, the mechanism by which Amot is targeted to endosomes is unknown. Here, a novel lipid binding domain within Amot is shown to selectively bind with high affinity to membranes containing monophosphorylated phosphatidylinositols and cholesterol. With similar lipid specificity, Amot inserts into and tubulates membranes in vitro and enlarges perinuclear endosomal compartments in cells. Based on the similar distribution of Amot with cholesterol, Rab11, and Arf6, such membrane interactions are identified at juxtanuclear endocytic recycling compartments. Taken together, these findings indicate that Amot is targeted along with associated apical polarity proteins to the endocytic recycling compartment via this novel membrane binding domain.

AB - Polarity proteins promote the asymmetric organization of cells by orienting intracellular sorting mechanisms, such as protein trafficking and cytoskeletal assembly. The localization of individual polarity proteins in turn is often determined by association with factors that mediate contact with other cells or the substratum. This arrangement for the Par and Crb apical polarity complexes at the tight junction is disrupted by the adaptor protein Amot. Amot directly binds the scaffolding proteins Patj and Mupp1 and redistributes them and their binding partners from the plasma membrane to endosomes. However, the mechanism by which Amot is targeted to endosomes is unknown. Here, a novel lipid binding domain within Amot is shown to selectively bind with high affinity to membranes containing monophosphorylated phosphatidylinositols and cholesterol. With similar lipid specificity, Amot inserts into and tubulates membranes in vitro and enlarges perinuclear endosomal compartments in cells. Based on the similar distribution of Amot with cholesterol, Rab11, and Arf6, such membrane interactions are identified at juxtanuclear endocytic recycling compartments. Taken together, these findings indicate that Amot is targeted along with associated apical polarity proteins to the endocytic recycling compartment via this novel membrane binding domain.

UR - http://www.scopus.com/inward/record.url?scp=77951228917&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77951228917&partnerID=8YFLogxK

U2 - 10.1074/jbc.M109.096230

DO - 10.1074/jbc.M109.096230

M3 - Article

C2 - 20080965

AN - SCOPUS:77951228917

VL - 285

SP - 12308

EP - 12320

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -