Dynein
class of enzymes
Dyneins are a family of cytoskeletal motor proteins (though they are actually protein complexes) that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport.
Classification
Dyneins can be divided into two groups: cytoplasmic dyneins and axonemal dyneins, which are also called ciliary or flagellar dyneins.
Cytoplasmic
Heavy chain: DYNC1H1, DYNC2H1
Intermediate chain: DYNC1I1, DYNC1I2
Light intermediate chain: DYNC1LI1, DYNC1LI2, DYNC2LI1
Light chain: DYNLL1, DYNLL2, DYNLRB1, DYNLRB2, DYNLT1, DYNLT3
Axonemal
Heavy chain: DNAH1, DNAH2, DNAH3, DNAH5, DNAH6, DNAH7, DNAH8, DNAH9, DNAH10, DNAH11, DNAH12, DNAH13, DNAH14, DNAH17
Intermediate chain: DNAI1, DNAI2
Light intermediate chain: DNALI1
Light chain: DNAL1, DNAL4
Function
Axonemal dynein causes sliding of microtubules in the axonemes of cilia and flagella and is found only in cells that have those structures.
Cytoplasmic dynein, found in all animal cells and possibly plant cells as well, performs functions necessary for cell survival such as organelle transport and centrosome assembly. Cytoplasmic dynein moves processively along the microtubule; that is, one or the other of its stalks is always attached to the microtubule so that the dynein can "walk" a considerable distance along a microtubule without detaching.
Cytoplasmic dynein helps to position the Golgi complex and other organelles in the cell.
This brief starts where responsible research should: with the source description of “Dynein” as class of enzymes. Everything that follows is an evidence route, not borrowed authority.
Why this record matters
The subject matters to the general reference register because the source frames it as class of enzymes. Its deeper value depends on whether names, dates, institutions and citations support that framing.
Named sources, stable identifiers and responsible institutions provide the strongest route from overview to verifiable evidence. The source revision retrieved here is dated Sep 16, 2026. The linked authority identifier is Q410134. None of the 0 selected statements returned an explicit reference.
Overview language is designed for orientation and should not be treated as a substitute for the evidence cited beneath it. The lead is largely declarative, so disagreement and counter-evidence require a deliberate search beyond the opening account. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.
How to read it
Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.
- Subject orientation
- Search vocabulary
- Locating named sources
The closest primary source, responsible institution and strongest cited specialist reference.
Three-step research path
- Establish the record: confirm the title “Dynein”, its source revision and the description used here.
- Expand the search: follow Dynein primary sources, Dynein archive and Dynein research across catalogues and specialist indexes.
- Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.
Questions for further research
- Which source most directly establishes the central claim about “Dynein”?
- What terminology or title could unlock a more precise catalogue search?
- Which cited source is closest to the event, object or claim?
Search terms from this dossier
This entry incorporates text from “Dynein” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.