Component
Beta-tubulin polyglutamylation in mouse TTLL7 assays
Context-specific entity; species, compartment and exposure are stated on each claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
Recombinant mouse TTLL7 favored beta-tubulin polyglutamylation in vitro and when expressed in HEK293T cells.
Experimental context and source evidence
- evidence_access
- Primary abstract and full-text construct methods
- experimental_model
- Mouse cDNA constructs, recombinant biochemistry and human host-cell expression.
- limitations
- This protein modification differs from a free-glutamate receptor signal; the beta-tubulin isoform is not assigned beyond the study.
- nutrient_topic
- L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
- plain_language
- Glutamate can be added in side chains that modify a structural protein.
- primary_references
- TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of MAP2-positive neurites. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16901895/ · DOI 10.1074/jbc.M603984200
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 410–416
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse cDNA constructs, recombinant biochemistry and human host-cell expression. · source_derived_draft · unverified_draft
## glutamate-tubulin-glutamylation Glutamate can be added in side chains that modify a structural protein. Recombinant mouse TTLL7 favored beta-tubulin polyglutamylation in vitro and when expressed in HEK293T cells. Model: Mouse cDNA constructs, recombinant biochemistry and human host-cell expression. Limitations: This protein modification differs from a free-glutamate receptor signal; the beta-tubulin isoform is not assigned beyond the study. Evidence access: Primary abstract and full-text construct methods TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of MAP2-positive neurites. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16901895/ · DOI 10.1074/jbc.M603984200
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.