- Interfilament binding of tethered molecules
Models of cellular contraction, for example, in striated muscle, usually involve mass action kinetics. Mijailovich et al. implement spatially explicit actomyosin interactions in the Monte Carlo platform MUSICO and show the extent to which myosin tethering affects other biological parameters.
- Separate activation of TMEM16A subunits
TMEM16 lipid scramblases are formed from two identical subunits, but the pore architecture of TMEM16 channels remains unclear. Jeng et al. use tandem dimers of TMEM16A subunits with different mutations and show that each subunit comprises an independent pore and contains more than one Ca2+-binding site.
- Hv1 mechanosensitivity
Hv1 is a voltage-gated proton channel that is composed of two voltage-sensing domains, each of which is permeable to protons. Pathak et al. find that these voltage-sensing domains are mechanosensitive and that membrane stretch results in a long-lived facilitation of Hv1 activation.
- Alcohol and BK channel gating
Large conductance K+ channels of the slo1 family are gated by Ca2+ and voltage and either inhibited or potentiated by ethanol. Kuntamallappanavar and Dopico analyze the effects of ethanol in detail and find that the absence or presence of β subunits leads to differential modification of channel gating parameters by intoxicating levels of ethanol.
- Independent activation of TMEM16A subunits
The TMEM16 family contains dimeric membrane proteins activated by intracellular Ca2+. Realizing that lipid scramblase family members contain two independently activated subunits, Lim et al. use concatenated TMEM16A subunits to show that ion channel members contain two independently activated pores.
- Structure of anthrax lethal toxin prepore complex
Anthrax toxin is a tripartite complex in which the protective antigen moiety forms a pore through which lethal factor and edema factor are translocated. Fabre et al. reveal a mechanism for efficient translocation in their structure of the heptameric protective antigen prepore bound to three lethal factors.