The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation

T Arnesen, KK Starheim, P Van Damme… - … and cellular biology, 2010 - Am Soc Microbiol
The human NatA protein N α-terminal-acetyltransferase complex is responsible for
cotranslational N-terminal acetylation of proteins with Ser, Ala, Thr, Gly, and Val N termini …

[HTML][HTML] Structure of human NatA and its regulation by the huntingtin interacting protein HYPK

L Gottlieb, R Marmorstein - Structure, 2018 - cell.com
Co-translational N-terminal protein acetylation regulates many protein functions including
degradation, folding, interprotein interactions, and targeting. Human NatA (hNatA), one of six …

[HTML][HTML] Structural basis of HypK regulating N-terminal acetylation by the NatA complex

FA Weyer, A Gumiero, K Lapouge, G Bange… - Nature …, 2017 - nature.com
In eukaryotes, N-terminal acetylation is one of the most common protein modifications
involved in a wide range of biological processes. Most N-acetyltransferase complexes …

[HTML][HTML] N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate

L Gottlieb, L Guo, J Shorter, R Marmorstein - Journal of Biological …, 2021 - ASBMB
Huntington's disease (HD) is a neurodegenerative disorder caused by a poly-CAG
expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine tract in …

[HTML][HTML] The human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4

K Hole, P Van Damme, M Dalva, H Aksnes… - PloS one, 2011 - journals.plos.org
Protein Nα-terminal acetylation (Nt-acetylation) is considered one of the most common
protein modification in eukaryotes, and 80-90% of all soluble human proteins are modified in …

[HTML][HTML] Human Naa50p (Nat5/San) displays both protein Nα-and Nϵ-acetyltransferase activity

R Evjenth, K Hole, OA Karlsen, M Ziegler… - Journal of Biological …, 2009 - ASBMB
Protein acetylation is a widespread modification that is mediated by site-selective
acetyltransferases. KATs (lysine N ϵ-acetyltransferases), modify the side chain of specific …

Chaperone protein HYPK interacts with the first 17 amino acid region of Huntingtin and modulates mutant HTT-mediated aggregation and cytotoxicity

KR Choudhury, NP Bhattacharyya - Biochemical and biophysical research …, 2015 - Elsevier
Huntington's disease is a polyglutamine expansion disorder, characterized by mutant HTT-
mediated aggregate formation and cytotoxicity. Many reports suggests roles of N-terminal 17 …

HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits …

S Raychaudhuri, M Sinha… - Human molecular …, 2008 - academic.oup.com
Expansion of polymorphic glutamine (Q) numbers present at the protein Huntingtin (Htt)
beyond 36Q results in its misfolding and aggregation, and the aggregates recruit several …

Cloning and characterization of hNAT5/hSAN: An evolutionarily conserved component of the NatA protein N-α-acetyltransferase complex

T Arnesen, D Anderson, J Torsvik, HB Halseth… - Gene, 2006 - Elsevier
The human hARD1–NATH complex, cotranslationally acetylating the α-amino groups of
proteins, was recently described. In S. cerevisiae and D. melanogaster this NatA complex …

[HTML][HTML] Crystal structure of the Golgi-associated human Nα-acetyltransferase 60 reveals the molecular determinants for substrate-specific acetylation

SI Støve, RS Magin, H Foyn, BE Haug, R Marmorstein… - Structure, 2016 - cell.com
N-Terminal acetylation is a common and important protein modification catalyzed by N-
terminal acetyltransferases (NATs). Six human NATs (NatA–NatF) contain one catalytic …