DYNLT2B, also known as TCTEX1D2, is a non-catalytic Tctex-family light chain of cytoplasmic dynein-2. It forms a heterodimer with DYNLT1 and associates with the intermediate-chain assembly to support retrograde intraflagellar transport and ciliary homeostasis. Human variants can disrupt retrograde transport, while mouse studies additionally identify a role in sperm-flagellum assembly.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000922 spindle pole | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | KEEP AS NON CORE | Summary: Spindle-pole localization was observed during cell division; this is a secondary localization alongside the core ciliary dynein-2 role. Reason: Spindle-pole localization was observed during cell division; this is a secondary localization alongside the core ciliary dynein-2 role. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells. |
| GO:0001673 male germ cell nucleus | NAS PMID:36973253 Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 reg... | UNDECIDED | Summary: The cited full text analyzes DYNLRB1/DYNLRB2 in mouse meiosis; it does not establish a DYNLT2B-specific male-germ-cell nuclear localization in the material examined. The precise target and localization evidence behind this NAS assignment remain unresolved. Reason: The cited full text analyzes DYNLRB1/DYNLRB2 in mouse meiosis; it does not establish a DYNLT2B-specific male-germ-cell nuclear localization in the material examined. The precise target and localization evidence behind this NAS assignment remain unresolved. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:26044572 TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dyst... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. Reason: The physical interaction is retained, but generic protein binding does not specify the dynein intermediate-chain interaction that defines the core mechanism. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: DYNLT2B is an intracellular non-motor subunit that assembles with dynein-2. Reason: DYNLT2B is an intracellular non-motor subunit that assembles with dynein-2. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0005813 centrosome | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: Centrosomal localization is supported by the human immunofluorescence experiments and is consistent with recruitment to the ciliary base. Reason: Centrosomal localization is supported by the human immunofluorescence experiments and is consistent with recruitment to the ciliary base. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells. |
| GO:0005868 cytoplasmic dynein complex | IBA GO_REF:0000033 | ACCEPT | Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0005868 cytoplasmic dynein complex | IDA PMID:25205765 Subunit composition of the human cytoplasmic dynein-2 comple... | ACCEPT | Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0005868 cytoplasmic dynein complex | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0005929 cilium | NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver... | ACCEPT | Summary: Dynein-2-dependent trafficking places the protein in the ciliary transport system, with direct localization strongest at the base. Reason: Dynein-2-dependent trafficking places the protein in the ciliary transport system, with direct localization strongest at the base. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. |
| GO:0005929 cilium | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | ACCEPT | Summary: Dynein-2-dependent trafficking places the protein in the ciliary transport system, with direct localization strongest at the base. Reason: Dynein-2-dependent trafficking places the protein in the ciliary transport system, with direct localization strongest at the base. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. |
| GO:0005930 axoneme | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | KEEP AS NON CORE | Summary: Axonemal signal was observed for overexpressed tagged TCTEX1D2; the same study did not detect a clear endogenous axonemal signal. Retain the experimental localization with this limitation. Reason: Axonemal signal was observed for overexpressed tagged TCTEX1D2; the same study did not detect a clear endogenous axonemal signal. Retain the experimental localization with this limitation. Supporting Evidence: PMID:25830415 overexpression of LAP(EGFP-TEV-S-Peptide)-Tctex1d2 led to the localization of LAP-Tctex1d2 to the ciliary axoneme (Fig. 3I), similar to what had been observed with Wdr60 overexpression.4 |
| GO:0007018 microtubule-based movement | IBA GO_REF:0000033 | ACCEPT | Summary: The light chain participates in microtubule-based movement as an accessory part of the dynein-2 transport machinery. Reason: The light chain participates in microtubule-based movement as an accessory part of the dynein-2 transport machinery. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0030286 dynein complex | NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver... | MODIFY | Summary: The established human complex is cytoplasmic dynein-2, rather than an unspecified dynein complex. Reason: The established human complex is cytoplasmic dynein-2, rather than an unspecified dynein complex. Proposed replacements: cytoplasmic dynein complex Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0030286 dynein complex | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | MODIFY | Summary: The established human complex is cytoplasmic dynein-2, rather than an unspecified dynein complex. Reason: The established human complex is cytoplasmic dynein-2, rather than an unspecified dynein complex. Proposed replacements: cytoplasmic dynein complex Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:0031021 interphase microtubule organizing center | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | KEEP AS NON CORE | Summary: The interphase microtubule-organizing-center localization is directly observed, but its role is less specific than ciliary-base recruitment. Reason: The interphase microtubule-organizing-center localization is directly observed, but its role is less specific than ciliary-base recruitment. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells. |
| GO:0035721 intraciliary retrograde transport | IMP PMID:29742051 Interaction of WDR60 intermediate chain with TCTEX1D2 light ... | ACCEPT | Summary: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Reason: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. |
| GO:0035721 intraciliary retrograde transport | NAS PMID:31451806 Structure of the dynein-2 complex and its assembly with intr... | ACCEPT | Summary: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Reason: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. |
| GO:0035721 intraciliary retrograde transport | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | ACCEPT | Summary: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Reason: Human TCTEX1D2 knockout cells exhibit defects in retrograde ciliary protein trafficking; the auxiliary role is directly supported. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. |
| GO:0045505 dynein intermediate chain binding | IBA GO_REF:0000033 | ACCEPT | Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3. |
| GO:0045505 dynein intermediate chain binding | IPI PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3. |
| GO:0045505 dynein intermediate chain binding | IPI PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3. |
| GO:0060271 cilium assembly | IMP PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: Depletion impairs ciliogenesis in the human cell assay. Phenotype severity varies with assay and cell context, so this does not mean every cilium requires an identical absolute amount of DYNLT2B. Reason: Depletion impairs ciliogenesis in the human cell assay. Phenotype severity varies with assay and cell context, so this does not mean every cilium requires an identical absolute amount of DYNLT2B. Supporting Evidence: PMID:25830415 Tctex1d2 and Wdr60 localize to the base of the cilium and their depletion causes defects in ciliogenesis. |
| GO:0097546 ciliary base | IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot... | ACCEPT | Summary: Human microscopy places endogenous TCTEX1D2 at the ciliary base, consistent with dynein-2 recruitment. Reason: Human microscopy places endogenous TCTEX1D2 at the ciliary base, consistent with dynein-2 recruitment. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells. |
| GO:0120293 dynein axonemal particle | IEA GO_REF:0000044 | UNDECIDED | Summary: The available studies establish dynein-2 membership and ciliary-base localization, but do not directly establish residence in a dynein axonemal particle. Axoneme, axonemal dynein, and assembly-particle localization are distinct claims. Reason: The available studies establish dynein-2 membership and ciliary-base localization, but do not directly establish residence in a dynein axonemal particle. Axoneme, axonemal dynein, and assembly-particle localization are distinct claims. |
| GO:1902017 regulation of cilium assembly | IMP PMID:25205765 Subunit composition of the human cytoplasmic dynein-2 comple... | ACCEPT | Summary: TCTEX1D2 affects ciliary assembly and homeostasis through its accessory role in the dynein-2 machinery. Reason: TCTEX1D2 affects ciliary assembly and homeostasis through its accessory role in the dynein-2 machinery. Supporting Evidence: PMID:25205765 We show that the proteins encoded by the ciliopathy genes WDR34 and WDR60 are bona fide dynein-2 intermediate chains and are both required for dynein-2 function. In addition, we identify TCTEX1D2 as a unique dynein-2 light chain that is itself required for cilia function. |
| GO:1905799 regulation of intraciliary retrograde transport | IMP PMID:26044572 TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dyst... | ACCEPT | Summary: Loss of TCTEX1D2 destabilizes the retrograde IFT motor and impairs retrograde transport, supporting a regulatory contribution. Reason: Loss of TCTEX1D2 destabilizes the retrograde IFT motor and impairs retrograde transport, supporting a regulatory contribution. Supporting Evidence: PMID:26044572 Loss of TCTEX1D2 impairs retrograde intraflagellar transport (IFT) in humans and the protist Chlamydomonas, accompanied by destabilization of the retrograde IFT dynein motor. We thus define TCTEX1D2 as an integral component of the evolutionarily conserved retrograde IFT machinery. |
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