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Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

Pilt is a coiled-coil domain-containing protein that localizes at the trans-Golgi complex and regulates its structure

Hideaki Tamaki1, Masashi Sanda, Osamu Katsumata

  • 1Department of Anatomy, Kitasato University School of Medicine, Sagamihara 252-0374, Japan.

FEBS Letters
|July 31, 2012
PubMed

Insights

Protein incorporated later into tight junctions (Pilt) is crucial for maintaining Golgi structure. This Arf6-binding protein

Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Protein incorporated later into tight junctions (Pilt), also known as tight junction-associated protein 1 or tight junction protein 4, is a coiled-coil domain-containing protein.
  • Pilt was initially identified as a human discs large-interacting protein.

Purpose of the Study:

  • To identify novel binding partners of Arf6.
  • To investigate the cellular localization and function of Pilt.

Main Methods:

  • Yeast two-hybrid screening to identify Arf6-binding proteins.
  • Immunocytochemical analysis to determine Pilt localization in NIH3T3 cells.
  • Endogenous Pilt silencing to assess its effect on cellular structures.

Main Results:

  • Pilt was identified as an Arf6-binding protein.
  • Pilt predominantly localizes to the trans-Golgi complex, with diffuse cytoplasmic distribution associated with endosomes and the plasma membrane.
  • Silencing of endogenous Pilt led to disruption of the Golgi structure.

Conclusions:

  • Pilt plays a significant role in the maintenance of Golgi structure.
  • The findings suggest a functional involvement of Pilt in Golgi organization and dynamics.

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