Exposure of phosphatidylserine on the cell surface

S Nagata, J Suzuki, K Segawa, T Fujii - Cell Death & Differentiation, 2016 - nature.com
Phosphatidylserine (PtdSer) is a phospholipid that is abundant in eukaryotic plasma
membranes. An ATP-dependent enzyme called flippase normally keeps PtdSer inside the …

Structure and function of TMEM16 proteins (anoctamins)

N Pedemonte, LJV Galietta - Physiological reviews, 2014 - journals.physiology.org
TMEM16 proteins, also known as anoctamins, are involved in a variety of functions that
include ion transport, phospholipid scrambling, and regulation of other membrane proteins …

X-ray structure of a calcium-activated TMEM16 lipid scramblase

JD Brunner, NK Lim, S Schenck, A Duerst, R Dutzler - Nature, 2014 - nature.com
The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional
diversity. This family contains the long sought-after Ca2+-activated chloride channels as well …

[HTML][HTML] The groovy TMEM16 family: molecular mechanisms of lipid scrambling and ion conduction

V Kalienkova, VC Mosina, C Paulino - Journal of Molecular Biology, 2021 - Elsevier
The TMEM16 family of membrane proteins displays a remarkable functional dichotomy–
while some family members function as Ca 2+-activated anion channels, the majority of …

Mutations in ANO3 cause dominant craniocervical dystonia: ion channel implicated in pathogenesis

G Charlesworth, V Plagnol, KM Holmström… - The American Journal of …, 2012 - cell.com
In this study, we combined linkage analysis with whole-exome sequencing of two individuals
to identify candidate causal variants in a moderately-sized UK kindred exhibiting autosomal …

Anoctamins/TMEM16 proteins: chloride channels flirting with lipids and extracellular vesicles

JM Whitlock, HC Hartzell - Annual review of physiology, 2017 - annualreviews.org
Anoctamin (ANO)/TMEM16 proteins exhibit diverse functions in cells throughout the body
and are implicated in several human diseases. Although the founding members ANO1 …

Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A

C Paulino, Y Neldner, AKM Lam, V Kalienkova… - elife, 2017 - elifesciences.org
The calcium-activated chloride channel TMEM16A is a member of a conserved protein
family that comprises ion channels and lipid scramblases. Although the structure of the …

Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM

V Kalienkova, V Clerico Mosina, L Bryner… - Elife, 2019 - elifesciences.org
Scramblases catalyze the movement of lipids between both leaflets of a bilayer. Whereas
the X-ray structure of the protein nhTMEM16 has previously revealed the architecture of a …

Explaining calcium-dependent gating of anoctamin-1 chloride channels requires a revised topology

K Yu, C Duran, Z Qu, YY Cui, HC Hartzell - Circulation research, 2012 - Am Heart Assoc
Rationale: Ca2+-activated Cl channels play pivotal roles in the cardiovascular system. They
regulate vascular smooth muscle tone and participate in cardiac action potential …

Physiological roles and diseases of Tmem16/Anoctamin proteins: are they all chloride channels?

C Duran, H Hartzell - Acta pharmacologica Sinica, 2011 - nature.com
The Tmem16 gene family was first identified by bioinformatic analysis in 2004. In 2008, it
was shown independently by 3 laboratories that the first two members (Tmem16A and …