Related Experiment Video
Updated: Jun 23, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Rich can get poor: conversion of hub to non-hub proteins
Kyaw Tun1, Raghuraj Keshava Rao, Lakshminarayanan Samavedham
1Synthetic Biology Lab, RIKEN Advanced Sciences Institute, 1-7-22, Suehiro-cho, Tsurumi, 230-0045, Yokohama, Japan, kyawtun@gsc.riken.jp.
Abstract:
Hubs are ubiquitous network elements with high connectivity. One of the common observations about hub proteins is their preferential attachment leading to scale-free network topology. Here we examine the question: does rich protein always get richer, or can it get poor too? To answer this question, we compared similar and well-annotated hub proteins in six organisms, from prokaryotes to eukaryotes. Our findings indicate that hub proteins retain, gain or lose connectivity based on the context. Furthermore, the loss or gain of connectivity appears to correlate with the functional role of the protein in a given system.
Related Concept Videos
Export of Misfolded Proteins out of the ER
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation
Transcription is the synthesis of RNA molecules by RNA...
Conservation of Protein Domains
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
