Ligand binding to the ACBD6 protein regulates the acyl-CoA transferase reactions in membranes

Soupène, Eric; Kuypers, Frans A.

doi:10.1194/jlr.m061937

Cited by 21 publications

(36 citation statements)

References 50 publications

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“…As previously reported ( 18,19 ), ACBD6 (32 kDa) behaved as a monomeric protein, and no high molecular mass species were detected after DSS treatment ( Fig. 3A ).…”

Section: Acbd6 and Nmt2 Form Hetero-dimeric Complexessupporting

confidence: 52%

“…ACBD6 binds C 18:2 -CoA with greater affi nity than C 16 -CoA ( 18,19 ). At an equal concentration of C 18:2 -CoA and C 16 -CoA (5 M), ACBD6 could no longer prevent processing of C 16 -CoA by ecNMT2 and activity rate doubled ( Fig.…”

Section: Displacement Of C 16 -Coa By Linoleoyl-coamentioning

confidence: 99%

“…Ellman's reagent by guest, on www.jlr.org Supplemental Material can be found at: 19 ). All experiments were performed in ammonium acetate (25 mM, pH 7.4), supplemented with 0.1% Triton X-100 to prevent precipitation of ecNMT2, at 30°C.…”

Section: Methodsmentioning

confidence: 99%

“…Under similar conditions, addition of purifi ed ACBD1 had only a weak stimulatory effect. Compared with ACBD6, two ACBD6 mutant forms, Y 114 A and FKKY-AAAA (dubbed FKKY mut ), with defects in acyl-CoA binding ( 19 ) failed to stimulate the reaction in the presence of C 14 -CoA, thus acyl-CoA binding of ACBD6 is required for the stimulatory effect on NMT2 activity ( Fig. 5 ).…”

Section: Ligand Binding To Acbd6 Stimulates the Nmt Reactionmentioning

confidence: 99%

“…Cloning of human ACBD1 and ACBD6 was previously reported ( 18,19 ). Human NMT2 isoform 1 (NP_004799) was cloned by PCR from NM_004808.2 into pBIND vector and human ACBD6 was cloned into the pACT vector (Check-Mate Mammalian twohybrid system; Promega).…”

Section: Cloning and Site-directed Mutagenesismentioning

confidence: 99%

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Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA

Soupène¹,

Kao²,

Cheng³

et al. 2016

Journal of Lipid Research

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“…As previously reported ( 18,19 ), ACBD6 (32 kDa) behaved as a monomeric protein, and no high molecular mass species were detected after DSS treatment ( Fig. 3A ).…”

Section: Acbd6 and Nmt2 Form Hetero-dimeric Complexessupporting

confidence: 52%

Section: Displacement Of C 16 -Coa By Linoleoyl-coamentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Ligand Binding To Acbd6 Stimulates the Nmt Reactionmentioning

confidence: 99%

Section: Cloning and Site-directed Mutagenesismentioning

confidence: 99%

See 3 more Smart Citations

Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA

Soupène¹,

Kao²,

Cheng³

et al. 2016

Journal of Lipid Research

Self Cite

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ACBD3 functions as a scaffold to organize the Golgi stacking proteins and a Rab33b‐GAP

et al. 2017

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Golgin45 plays important roles in Golgi stack assembly and is known to bind both the Golgi stacking protein GRASP55 and Rab2 in the medial-Golgi cisternae. In this study, we sought to further characterize the cisternal adhesion complex using a proteomics approach. We report here that Acyl-CoA binding domain containing 3 (ACBD3) is likely to be a novel binding partner of Golgin45. ACBD3 interacts with Golgin45 via its GOLD domain, while its co-expression significantly increases Golgin45 targeting to the Golgi. Furthermore, ACBD3 recruits TBC1D22, a Rab33b GTPase activating protein (GAP), to a large multi-protein complex containing Golgin45 and GRASP55. These results suggest that ACBD3 may provide a scaffolding to organize the Golgi stacking proteins and a Rab33b-GAP at the medial-Golgi.

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A gold revision of the Golgi Dynamics (GOLD) domain structure and associated cell functionalities

Mendes

Costa-Filho

2022

FEBS Letters

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The classical secretory pathway is the key membrane-based delivery system in eukaryotic cells. Several families of proteins involved in the secretory pathway, with functionalities going from cargo sorting receptors to the maintenance and dynamics of secretory organelles, share soluble globular domains predicted to mediate protein-protein interactions. One of them is the 'Golgi Dynamics' (GOLD) domain, named after its strong association with the Golgi apparatus. There are many GOLD-containing protein families, such as the transmembrane emp24 domain-containing proteins (TMED/p24 family), animal SEC14-like proteins, human Golgi resident protein ACBD3, a splice variant of TICAM2 called TRAM with GOLD domain, and FYCO1. Here, we critically review the state-of-the-art knowledge of the structures and functions of the main representatives of GOLD-containing proteins in vertebrates. We provide the first unified description of the GOLD domain structure across different families since the first high-resolution structure was determined. With a brand-new update on the definition of the GOLD domain, we also discuss how its tertiary structure fits the b-sandwich-like fold map and give exciting new directions for forthcoming studies.

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Ligand binding to the ACBD6 protein regulates the acyl-CoA transferase reactions in membranes

Cited by 21 publications

References 50 publications

Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA

Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA

ACBD3 functions as a scaffold to organize the Golgi stacking proteins and a Rab33b‐GAP

A gold revision of the Golgi Dynamics (GOLD) domain structure and associated cell functionalities

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