Title | Redefining the BH3 Death Domain as a 'Short Linear Motif'. |
Publication Type | Journal Article |
Year of Publication | 2015 |
Authors | Aouacheria, A., C. Combet, P. Tompa, and M. J Hardwick |
Journal | Trends Biochem Sci |
Volume | 40 |
Issue | 12 |
Pagination | 736-48 |
Date Published | 2015 Dec |
ISSN | 0968-0004 |
Keywords | Amino Acid Motifs, Animals, BH3 Interacting Domain Death Agonist Protein, Humans, Models, Molecular, Protein Conformation |
Abstract | B cell lymphoma-2 (BCL-2)-related proteins control programmed cell death through a complex network of protein-protein interactions mediated by BCL-2 homology 3 (BH3) domains. Given their roles as dynamic linchpins, the discovery of novel BH3-containing proteins has attracted considerable attention. However, without a clearly defined BH3 signature sequence the BCL-2 family has expanded to include a nebulous group of nonhomologous BH3-only proteins, now justified by an intriguing twist. We present evidence that BH3s from both ordered and disordered proteins represent a new class of short linear motifs (SLiMs) or molecular recognition features (MoRFs) and are diverse in their evolutionary histories. The implied corollaries are that BH3s have a broad phylogenetic distribution and could potentially bind to non-BCL-2-like structural domains with distinct functions. |
DOI | 10.1016/j.tibs.2015.09.007 |
Alternate Journal | Trends Biochem. Sci. |
PubMed ID | 26541461 |
PubMed Central ID | PMC5056427 |
Grant List | DP2 NS083372 / NS / NINDS NIH HHS / United States R01 GM077875 / GM / NIGMS NIH HHS / United States R01 NS037402 / NS / NINDS NIH HHS / United States R01 NS083372 / NS / NINDS NIH HHS / United States |
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