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Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Updated: Jul 3, 2026

Studying Protein Function and the Role of Altered Protein Expression by Antibody Interference and Three-dimensional Reconstructions
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Published on: April 21, 2016

A small molecule-directed approach to control protein localization and function.

Prasanthi Geda1, Srikanth Patury, Jun Ma

  • 1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-2216, USA.

Yeast (Chichester, England)
|August 1, 2008
PubMed
Summary
This summary is machine-generated.

Researchers developed a rapamycin-inducible system in yeast to control protein localization and function on demand. This method enables rapid, reversible manipulation for creating conditional mutants and studying protein roles.

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Yeast Genetics

Background:

  • Protein localization is a critical determinant of protein function and cellular activity.
  • Controlling protein localization offers a powerful way to regulate protein function.
  • Existing methods for controlling protein localization are often limited or lack temporal precision.

Purpose of the Study:

  • To develop a general, inducible system for controlling protein localization in budding yeast.
  • To enable on-demand manipulation of protein function through chemical stimulus.
  • To create conditional loss-of-function mutants and uncouple localization from endogenous signaling.

Main Methods:

  • Utilized rapamycin, a small molecule, to recruit a cellular address signal to target proteins.
  • Induced rapid and reversible nucleo-cytoplasmic transport of proteins.
  • Applied the system to study essential transcription factors like Hsf1p and Crz1p.

Main Results:

  • Demonstrated rapamycin-induced protein relocalization within 10-12 minutes, with reversibility upon drug removal.
  • Successfully mimicked an hsf1 mutant phenotype by inducing nuclear export of Hsf1p.
  • Showed that nuclear import of Crz1p alone is insufficient for transcriptional activity.

Conclusions:

  • The rapamycin-inducible localization system provides a powerful platform for generating conditional alleles in yeast.
  • This technology facilitates directed mislocalization studies and functional analysis of proteins.
  • The approach has potential for genome-wide applications in understanding protein function.