Insights into the regulation of cellular Mn2+ homeostasis via TMEM165

Vicogne, Dorothée; Beauval, Nicolas; Durin, Zoé; Allorge, Delphine; Kondratska, Kateryna; Haustrate, Aurélien; Prevarskaya, Natasha; Lupashin, Vladimir; Legrand, Dominique; Foulquier, François

doi:10.1016/j.bbadis.2023.166717

Cited by 6 publications

(1 citation statement)

References 44 publications

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“…In yeast, Gdt1p mediates Mn influx into the Golgi to activate metalloenzymes functioning in protein glycosylation 91 – 93 . The human ortholog TMEM165 has a similar role as Gdt1p and missense mutations are associated with congenital disorders of glycosylation (CDG) 91 , 94 – 96 . These transporters all help ensure that enzymes exported from the cytosol or embedded in membranes are appropriately metalated.…”

Section: Discussionmentioning

confidence: 99%

TerC proteins function during protein secretion to metalate exoenzymes

He,

Sachla,

Helmann

2023

Nat Commun

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Cytosolic metalloenzymes acquire metals from buffered intracellular pools. How exported metalloenzymes are appropriately metalated is less clear. We provide evidence that TerC family proteins function in metalation of enzymes during export through the general secretion (Sec-dependent) pathway. Bacillus subtilis strains lacking MeeF(YceF) and MeeY(YkoY) have a reduced capacity for protein export and a greatly reduced level of manganese (Mn) in the secreted proteome. MeeF and MeeY copurify with proteins of the general secretory pathway, and in their absence the FtsH membrane protease is essential for viability. MeeF and MeeY are also required for efficient function of the Mn2+-dependent lipoteichoic acid synthase (LtaS), a membrane-localized enzyme with an extracytoplasmic active site. Thus, MeeF and MeeY, representative of the widely conserved TerC family of membrane transporters, function in the co-translocational metalation of Mn2+-dependent membrane and extracellular enzymes.

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