Sorting the nuclear proteome.

ABSTRACT:

Motivation

Quantitative experimental analyses of the nuclear interior reveal a morphologically structured yet dynamic mix of membraneless compartments. Major nuclear events depend on the functional integrity and timely assembly of these intra-nuclear compartments. Yet, unknown drivers of protein mobility ensure that they are in the right place at the time when they are needed.

Results

This study investigates determinants of associations between eight intra-nuclear compartments and their proteins in heterogeneous genome-wide data. We develop a model based on a range of candidate determinants, capable of mapping the intra-nuclear organization of proteins. The model integrates protein interactions, protein domains, post-translational modification sites and protein sequence data

SUBMITTER: Bauer DC 

PROVIDER: S-EPMC3117375 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature