|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|
|Date Published||2015 Dec|
|Keywords||Amino Acid Motifs, Animals, BH3 Interacting Domain Death Agonist Protein, Humans, Models, Molecular, Protein Conformation|
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.
|Alternate Journal||Trends Biochem. Sci.|
|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
Redefining the BH3 Death Domain as a 'Short Linear Motif'.