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First-pass extracted concept

HcCCR

Candidate: toolkit item1 source documents10 linked claims
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Aliases

cation channelrhodopsin

Extracted Explainers

What the tool is doing

HcCCR is a Hyphochytrium catenoides channelrhodopsin described as an emerging optogenetic tool for controlling neurons and cardiomyocytes. The paper uses it as a closely homologous comparator to HcKCR1 with strongly different K+/Na+ permeability.

Source 1DOIPubMed

What problem it solves

It helps define how BR-like gating chemistry can support a channelrhodopsin with contrasting ion selectivity. As a tool, it expands the set of light-gated cation channels relevant to optogenetics.

Source 1DOIPubMed

What it does not solve

The abstract does not provide detailed application benchmarks in biological preparations. It also reports that the D116N mutation abolishes channel activity.

Source 1DOIPubMed

Alternatives

The main alternative/comparator in the abstract is HcKCR1, with additional family-level comparisons to GtCCR2 and RaCCR1.

Source 1DOIPubMed

Evidence Snippets

HcCCR (cation channelrhodopsin) ... [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 completely abolishes HcCCR channel activity.