LITERATURE · PEER REVIEWED

Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop

Structure · 2019 · Peer reviewed

COMPLETE CITATION

Citation and identifiers

Lee Y, Yoon E, Cho S, et al.. “Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop.” Structure. 27(5):846–852.e3 · doi:10.1016/j.str.2019.01.016.

PubMed ID
30827841

RESEARCH QUESTION

How does MRG15 binding release ASH1L autoinhibition and activate H3K36 methyltransferase activity?

The purified-complex structure and biochemistry explain catalytic activation by MRG15 but do not establish the consequence of an individual human variant.

INTERPRETATION BOUNDARY

Read the finding and limit together.

What this study supports

Structural work defined how MRG15 binding releases ASH1L catalytic autoinhibition and activates its H3K36 methyltransferase function.

What it cannot establish

Purified-complex structure and biochemistry do not establish the functional consequence of an individual human variant or a clinical severity relationship.

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