| Subunit type | *C. elegans* gene name | Human ortholog | Role in complex | Key references |
|---|---|---|---|---|
| Heavy chain | **che-3** | **DYNC2H1** | Core dynein-2 motor subunit; provides the ATPase/motor domain that powers retrograde intraflagellar transport (IFT) from ciliary tip to base. In *C. elegans*, CHE-3 is the essential conventional IFT-dynein heavy chain; in human dynein-2, two DYNC2H1 heavy chains form the motor core. (pqac-00000001, pqac-00000009, pqac-00000010) | Hao et al. 2011; Qiu et al. 2022; Hiyamizu et al. 2023 (pqac-00000001, pqac-00000009, pqac-00000010) |
| Light intermediate chain | **xbx-1** | **DYNC2LI1** | Dynein-2 light intermediate chain; binds the N-terminal/nonmotor tail of DYNC2H1 and helps bridge the heavy chain to intermediate-chain modules. In *C. elegans*, XBX-1 is an essential component of IFT-dynein required for retrograde IFT and cilia assembly. In human dynein-2, DYNC2LI1 is part of the DYNC2H1-DYNC2LI1 core subcomplex; the human complex has a reported **2:2:1:1 stoichiometry for DYNC2H1:DYNC2LI1:WDR60:WDR34**. (pqac-00000001, pqac-00000009, pqac-00000033, pqac-00000036) | Hao et al. 2011; Qiu et al. 2022; Hiyamizu et al. 2023 (pqac-00000001, pqac-00000009, pqac-00000033, pqac-00000036) |
| Intermediate chain | No clearly established named equivalent in the retrieved *C. elegans* xbx-1-focused literature | **WDR60 (DYNC2I1)** | One of the two dynein-2 intermediate chains. Associates with the DYNC2H1-DYNC2LI1 core through WD40-domain interactions and contributes to assembly of the heteromeric dynein-2 tail; also mediates functionally important interactions with IFT-B subunits such as IFT54. (pqac-00000010, pqac-00000012, pqac-00000034, pqac-00000035) | Tsurumi et al. 2019; Hiyamizu et al. 2023 (pqac-00000010, pqac-00000012, pqac-00000034, pqac-00000035) |
| Intermediate chain | No clearly established named equivalent in the retrieved *C. elegans* xbx-1-focused literature | **WDR34 (DYNC2I2)** | Second dynein-2 intermediate chain. Works with WDR60 to organize the asymmetric tail region of dynein-2; associates with light-chain arrays and is required for proper dynein-2 assembly and retrograde ciliary trafficking. (pqac-00000009, pqac-00000010, pqac-00000034, pqac-00000035) | Qiu et al. 2022; Tsurumi et al. 2019; Hiyamizu et al. 2023 (pqac-00000009, pqac-00000010, pqac-00000034, pqac-00000035) |
| Light chain | **dylt-1 / dylt-2** | **DYNLT family / TCTEX1D2-associated light-chain module** | Tctex-type light chains associated with the dynein-2 complex in *C. elegans*; bidirectional IFT behavior supports their participation in the IFT-dynein motor. In vertebrate/human dynein-2, TCTEX1D2 is a dynein-2-specific light chain associated with the WDR60 module. (pqac-00000013, pqac-00000010, pqac-00000034) | Hao et al. 2011; Tsurumi et al. 2019; Hiyamizu et al. 2023 (pqac-00000013, pqac-00000010, pqac-00000034) |
| Light chain | **dyrb-1** | **DYNLRB1 / DYNLRB2** | Roadblock-type light chain associated with IFT-dynein in *C. elegans*; contributes to dynein-2 light-chain architecture. In human dynein-2, roadblock-family dimers are incorporated into the intermediate-chain/light-chain modules. (pqac-00000013, pqac-00000010, pqac-00000034, pqac-00000036) | Hao et al. 2011; Tsurumi et al. 2019; Hiyamizu et al. 2023 (pqac-00000013, pqac-00000010, pqac-00000034, pqac-00000036) |
| Light chain | Various/not clearly resolved in the retrieved *C. elegans* xbx-1-focused literature | **DYNLL1 / DYNLL2** | LC8-family light chains that help heterodimerize and stabilize intermediate-chain subcomplexes in human dynein-2, especially the WDR34-associated module. Specific *C. elegans* one-to-one orthology was not clearly established in the retrieved evidence set. (pqac-00000010, pqac-00000034, pqac-00000036) | Tsurumi et al. 2019; Hiyamizu et al. 2023 (pqac-00000010, pqac-00000034, pqac-00000036) |


*Table: This table compares the dynein-2 complex across *C. elegans* and humans, highlighting where xbx-1/DYNC2LI1 fits within the motor. It is useful for linking worm functional genetics to current structural and ciliopathy-focused understanding of human dynein-2.*