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First-pass extracted concept

HcKCR1

Candidate: toolkit item1 source documents10 linked claims
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Aliases

kalium channelrhodopsin 1

Extracted Explainers

What the tool is doing

HcKCR1 is a channelrhodopsin from Hyphochytrium catenoides described as an emerging optogenetic tool for controlling neurons and cardiomyocytes. In this paper it is analyzed as a light-gated cation-conducting channel with distinctive K+/Na+ selectivity and BR-like gating intermediates.

Source 1DOIPubMed

What problem it solves

It offers a natural light-gated channelrhodopsin relevant to optogenetic control, especially in the context of potassium-selective conductance. The study also uses it to clarify how gating and selectivity are mechanistically coupled.

Source 1DOIPubMed

What it does not solve

The abstract does not establish full application performance boundaries in cells or animals. It also shows that the D116N mutation compromises its potassium-selective behavior by converting it into a weak Na+ channel.

Source 1DOIPubMed

Alternatives

The paper directly contrasts HcKCR1 with the closely homologous HcCCR, and also compares family-level behavior with GtCCR2 and RaCCR1.

Source 1DOIPubMed

Evidence Snippets

HcKCR1 (kalium channelrhodopsin 1) ... [is an] emerging optogenetic tool[] for controlling neurons and cardiomyocytes.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1application rolesupports2026Source 1DOIPubMed

HcKCR1 and HcCCR are emerging optogenetic tools for controlling neurons and cardiomyocytes.

Claim 2comparative mechanismsupports2026Source 1DOIPubMed

HcCCR does not exhibit outwardly directed active proton transfer, unlike HcKCR1 during the M2 state.

Claim 3comparative propertysupports2026Source 1DOIPubMed

HcKCR1 and HcCCR exhibit more than 100-fold different relative K+/Na+ permeabilities.

Claim 4kinetic relationshipsupports2026Source 1DOIPubMed

In Na+-selective variants, M2 rise coincides with the slow phase of M1 formation and channel opening, whereas in HcKCR1 and its mutants M2 is delayed.

Claim 5mechanismsupports2026Source 1DOIPubMed

Channel gating involves transfer of a proton from Asp116 to an unidentified residue located on the cytoplasmic side of the molecule.

Claim 6mechanismsupports2026Source 1DOIPubMed

The M1 state is subsequently converted into an M2 state that absorbs at approximately 400 nm.

Claim 7mechanismsupports2026Source 1DOIPubMed

The time course of Asp116-linked deprotonation correlates with channel opening.

Claim 8mechanismsupports2026Source 1DOIPubMed

The UV-absorbing product is a distinct M1 state with a deprotonated Schiff base that facilitates cation passage through the channel.

Claim 9mechanismsupports2026Source 1DOIPubMed

Wild-type HcKCR1 and HcCCR have an early far-UV-absorbing photocycle intermediate that precedes channel opening.

Claim 10mutation effectsupports2026Source 1DOIPubMed

The D116N mutation converts HcKCR1 into a weak Na+ channel.