It takes two to tango: the structure and function of LIM, RING, PHD and MYND domains

Jacqueline M Matthews, Mugdha Bhati, E Lehtomaki, R E Mansfield, Liza Cubeddu, Joel P Mackay

Research output: Contribution to journalArticleResearchpeer-review

58 Citations (Scopus)

Abstract

LIM (Lin-11, Isl-1, Mec-3), RING (Really interesting new gene), PHD (Plant homology domain) and MYND (myeloid, Nervy, DEAF-1) domains are all zinc-binding domains that ligate two zinc ions. Unlike the better known classical zinc fingers, these domains do not bind DNA, but instead mediate interactions with other proteins. LIM-domain containing proteins have diverse functions as regulators of gene expression, cell adhesion and motility and signal transduction. RING finger proteins are generally associated with ubiquitination; the presence of such a domain is the defining feature of a class of E3 ubiquitin protein ligases. PHD proteins have been associated with SUMOylation but most recently have emerged as a chromatin recognition motif that reads the methylation state of histones. The function of the MYND domain is less clear, but MYND domains are also found in proteins that have ubiquitin ligase and/or histone methyltransferase activity. Here we review the structure-function relationships for these domains and discuss strategies to modulate their activity.
Original languageEnglish
Pages (from-to)3681 - 3696
Number of pages16
JournalCurrent Pharmaceutical Design
Volume15
Issue number31
DOIs
Publication statusPublished - 2009
Externally publishedYes

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