TY - JOUR
T1 - The neuronal transcription factor Myt1L interacts via a conserved motif with the PAH1 domain of Sin3 to recruit the Sin3L/Rpd3L histone deacetylase complex
AU - Marcum, Ryan Dale
AU - Radhakrishnan, Ishwar
N1 - Funding Information:
This work was supported by grants from the American Heart Association to IR (17GRNT33680167) and RDM (16PRE27260041) and from an H-Foundation grant to IR awarded by the Robert H. Lurie Comprehensive Cancer Center at Northwestern University. We are grateful to Marius Wernig (Stanford) for providing Myt1L cDNA and to Yongbo Zhang for assistance with NMR data collection.
Funding Information:
This work was supported by grants from the American Heart Association to IR (17GRNT33680167) and RDM (16PRE27260041) and from an H‐Foundation grant to IR awarded by the Robert H. Lurie Comprehensive Cancer Center at Northwestern University. We are grateful to Marius Wernig (Stanford) for providing Myt1L cDNA and to Yongbo Zhang for assistance with NMR data collection.
Publisher Copyright:
© 2020 Federation of European Biochemical Societies
PY - 2020/7/1
Y1 - 2020/7/1
N2 - The Sin3L/Rpd3L histone deacetylase (HDAC) complex is one of six major HDAC complexes in the nucleus, and its recruitment by promoter-bound transcription factors is an important step in many gene transcription regulatory pathways. Here, we investigate how the Myt1L zinc finger transcription factor, important for neuronal differentiation and the maintenance of neuronal identity, recruits this complex at the molecular level. We show that Myt1L, through a highly conserved segment shared with its paralogs, interacts directly and specifically with the Sin3 PAH1 domain, binding principally to the canonical hydrophobic cleft found in paired amphipathic helix domain (PAH) domains. Our findings are relevant not only for other members of the Myt family but also for enhancing our understanding of the rules of protein–protein interactions involving Sin3 PAH domains.
AB - The Sin3L/Rpd3L histone deacetylase (HDAC) complex is one of six major HDAC complexes in the nucleus, and its recruitment by promoter-bound transcription factors is an important step in many gene transcription regulatory pathways. Here, we investigate how the Myt1L zinc finger transcription factor, important for neuronal differentiation and the maintenance of neuronal identity, recruits this complex at the molecular level. We show that Myt1L, through a highly conserved segment shared with its paralogs, interacts directly and specifically with the Sin3 PAH1 domain, binding principally to the canonical hydrophobic cleft found in paired amphipathic helix domain (PAH) domains. Our findings are relevant not only for other members of the Myt family but also for enhancing our understanding of the rules of protein–protein interactions involving Sin3 PAH domains.
KW - histone deacetylases
KW - neuronal differentiation
KW - repressor–corepressor interaction
KW - solution NMR spectroscopy
KW - structure–function analysis
KW - transcriptional repression
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U2 - 10.1002/1873-3468.13811
DO - 10.1002/1873-3468.13811
M3 - Article
C2 - 32391601
AN - SCOPUS:85085510461
VL - 594
SP - 2322
EP - 2330
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 14
ER -