Ontology highlight
ABSTRACT:
SUBMITTER: Dustrude ET
PROVIDER: S-EPMC5555265 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Dustrude Erik Thomas ET Perez-Miller Samantha S François-Moutal Liberty L Moutal Aubin A Khanna May M Khanna Rajesh R
Channels (Austin, Tex.) 20170228 4
The neuronal collapsin response mediator protein 2 (CRMP2) undergoes several posttranslational modifications that codify its functions. Most recently, CRMP2 SUMOylation (addition of small ubiquitin like modifier (SUMO)) was identified as a key regulatory step within a modification program that codes for CRMP2 interaction with, and trafficking of, voltage-gated sodium channel NaV1.7. In this paper, we illustrate the utility of combining sequence alignment within protein families with structural a ...[more]