homeoviscous adaptation
traitmech:000208 · CLASS · PROPOSED
A stress response in which an organism remodels membrane lipid composition to maintain a functional membrane viscosity and fluidity when temperature changes perturb lipid packing.
Trait evidence
-
DOI:10.1146/annurev-micro-091313-103612termed homeoviscous adaptation
-
DOI:10.1128/spectrum.03925-23Upon temperature decrease, the membrane rigidifies and increases in thickness, resulting in activation of the kinase-dominant state of DesK
-
DOI:10.1038/s41467-024-53677-5hard-wired parameters calibrate the system to generate membrane compositions that maintain constant fluidity
-
DOI:10.1038/s41467-024-53677-5restores optimal membrane fluidity within a single generation
Membrane-fluidity homeostasis by lipid remodeling
MECHANISTIC · This graph captures the conserved membrane-fluidity output of homeoviscous adaptation without making the Bacillus DesK/DesR two-component branch, E. coli FabI/FabB metabolic valve, or any single lipid species universal across microbes.
Edge evidence
-
temperature downshift
causes
membrane rigidification
biolink:causesA temperature decrease causes the bacterial membrane to rigidify and thicken.
-
DOI:10.1128/spectrum.03925-23Upon temperature decrease, the membrane rigidifies and increases in thickness
-
-
membrane rigidification
positively regulates
homeoviscous adaptation
RO:0002213Membrane rigidification is sensed as the physical input that activates homeoviscous lipid remodeling.
-
DOI:10.1128/spectrum.03925-23Upon temperature decrease, the membrane rigidifies and increases in thickness, resulting in activation of the kinase-dominant state of DesK
-
-
homeoviscous adaptation
positively regulates
membrane lipid remodeling
RO:0002213Homeoviscous adaptation increases lipid remodeling routes, including fatty-acyl desaturation, that counteract bilayer ordering.
-
DOI:10.1128/spectrum.03925-23desaturates the fatty acyl chains, resulting in membrane fluidization and concomitant decrease of bilayer thickness
-
-
FabI/FabB branchpoint enzymes
regulates
membrane lipid remodeling
RO:0002211The E. coli FabI/FabB branchpoint valve allocates fatty-acid synthesis flux between saturated and unsaturated membrane-lipid routes.
-
DOI:10.1038/s41467-024-53677-5A first element of this regulatory system is a temperature-sensitive metabolic valve that allocates flux between the saturated and unsaturated fatty acid synthesis pathways via the branchpoint enzymes FabI and FabB
-
-
membrane lipid remodeling
regulates
membrane fluidity
RO:0002211Temperature-dependent membrane lipid remodeling maintains membrane fluidity near a functional setpoint.
-
DOI:10.1038/s41467-024-53677-5hard-wired parameters calibrate the system to generate membrane compositions that maintain constant fluidity
-
-
membrane fluidity
contributes to
homeoviscous adaptation
RO:0002326Restoration of optimal membrane fluidity is the physiological output of homeoviscous adaptation.
-
DOI:10.1038/s41467-024-53677-5restores optimal membrane fluidity within a single generation
-
Protein and taxon examples
| Graph node | Protein | Taxon | UniProt status | Role and evidence |
|---|---|---|---|---|
| FabI/FabB branchpoint enzymes |
UniProtKB:P0AEK4
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI |
Escherichia coli K-12
NCBITaxon:83333
|
REVIEWED |
E. coli K-12 FabI catalyzes enoyl-ACP reduction in fatty-acid elongation and participates in the FabI/FabB metabolic valve that allocates flux between saturated and unsaturated fatty-acid synthesis during homeoviscous adaptation.
|
| FabI/FabB branchpoint enzymes |
UniProtKB:P0A953
3-oxoacyl-[acyl-carrier-protein] synthase 1 |
Escherichia coli K-12
NCBITaxon:83333
|
REVIEWED |
E. coli K-12 FabB elongates acyl-ACP substrates in fatty-acid biosynthesis and participates in the FabI/FabB metabolic valve that allocates flux between saturated and unsaturated fatty-acid synthesis during homeoviscous adaptation.
|
Provenance
- Identifier source
- TraitMech local identifier
- Definition source
DOI:10.1039/d4cc03114h
Parent traits (1)
Synonyms (2)
- homoviscous adaptation
- HVA
kg-microbe context
No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.
Canonical examples
-
Escherichia coli
NCBITaxon:562DOI:10.1038/s41467-024-53677-5 -
Bacillus subtilis
NCBITaxon:1423DOI:10.1128/spectrum.03925-23
Discussions and Knowledge Gaps
Resolve an exact external ontology class for organism-level homeoviscous adaptation before adding a TraitRecord xref.
No exact GO, PATO, or METPO class is present in the pinned local snapshot for homeoviscous adaptation. Related lipid metabolism, fatty-acid desaturation, membrane-fluidity, and cold-response terms are narrower, broader, or shifted from the whole-organism membrane-acclimation trait.
Curation history
-
·
MINTED_TRAITMECH_ID · codex
Minted homeoviscous adaptation as a DOI-backed stress-response TraitRecord after a repository-wide duplicate review covering ignored and hidden files; the local METPO snapshot has no exact homeoviscous-adaptation class and the replacement placeholder is reserved in proposals/metpo_traitmech_v85.
-
·
ADD_PROTEIN_EXAMPLES · codex
Added E. coli K-12 FabI and FabB UniProt protein examples to the homeoviscous adaptation causal graph and removed a top-level evidence item whose Maiti review citation had no verbatim snippet.
-
·
NORMALIZED_CAUSAL_NODE_ID · codex
Renamed the homeoviscous graph node membrane_rigidification to the canonical membrane_rigidity QUALITY node id after PR review found that the retired process-shaped alias had been reintroduced.