The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
BICD2 is not an enzyme or transporter. It is a cargo-selective, coiled-coil activating adaptor for cytoplasmic dynein-1 and dynactin. Its principal function is to connect selected cargos to the dynein–dynactin motor, convert that motor into a processive microtubule-minus-end-directed complex, and—in some settings—coordinate dynein with kinesin-1. The best-established cargos are Rab6-GTP-positive Golgi/secretory carriers, the nuclear-pore protein RanBP2/Nup358, and the outer-nuclear-membrane protein Nesprin-2. Thus, BICD2 acts mainly on cytoplasmic microtubules, at transport vesicles, and on the cytoplasmic face of the nuclear envelope. (splinter2012bicd2dynactinand pages 1-2, hoogenraad2016bicaudaldfamily pages 5-7, zhao2024molecularmechanismfor pages 1-2)
Recent work has clarified how BICD2 is switched between inactive and active conformations, how Rab6-GTP and Nup358 are recognized, and how CDK1–PLK1 phosphorylation activates a nuclear-envelope pool during G2/M. Pathogenic heterozygous variants cause a spectrum dominated by lower-extremity-predominant spinal muscular atrophy, but individual variants can affect different cargo interfaces and produce brain-developmental phenotypes. (yi2023roleofnesprin2 pages 2-4, gallisasune2023bicd2phosphorylationregulates pages 1-2, zhao2024molecularmechanismfor pages 1-2, gibson2023astructuralmodel pages 1-3)
The target is correctly identified as human BICD2, protein bicaudal D homolog 2/BICD cargo adaptor 2, UniProt Q8TD16. A vertebrate sequence alignment in the 2023 Nature Communications study explicitly labels the human BICD2 sequence as Q8TD16, and the literature describes the same protein as an approximately 94–95-kDa, 855-residue, elongated coiled-coil adaptor. The approved human target is also recorded as BICD2, ENSG00000185963, “BICD cargo adaptor 2.” (fagiewicz2022invitrocharacterization pages 1-4, OpenTargets Search: -BICD2, gallisasune2023bicd2phosphorylationregulates pages 4-5)
The architecture is consistent with the supplied UniProt/InterPro/Pfam assignment to the BicD family and BICD/PF09730 region: BICD2 contains three major coiled-coil regions, conventionally called CC1, CC2, and CC3, with the conserved C-terminal BICD cargo-binding region. The N-terminal half recruits dynein/dynactin, whereas the C terminus selects cargo and participates in autoinhibition. No conflicting human gene with the same symbol was encountered. Papers about Drosophila BicD or mammalian BICD1/BICDR proteins are ortholog/paralog evidence and are not treated here as direct evidence about Q8TD16 unless explicitly stated. (fagiewicz2022invitrocharacterization pages 1-4, gallisasune2023bicd2phosphorylationregulates pages 1-2, hoogenraad2016bicaudaldfamily pages 4-5)
BICD2 is a molecular scaffold and allosteric activator, not the ATP-hydrolyzing motor itself. Cytoplasmic dynein supplies ATPase activity and force; BICD2 supplies cargo specificity and stabilizes assembly of dynein with dynactin. Its elongated N-terminal coiled coil runs along the dynactin Arp1 filament and helps position the dynein tail, generating a processive dynein–dynactin–BICD2 complex. Reconstitution and single-molecule work showed stable ternary-complex formation and highly processive movement toward microtubule minus ends. (splinter2012bicd2dynactinand pages 1-2, hoogenraad2016bicaudaldfamily pages 4-5, hoogenraad2016bicaudaldfamily pages 5-7)
Dynein’s light intermediate chain provides an important direct contact: a conserved transient helix in LIC1/LIC2 binds the N-terminal region of BICD2 and other activating adaptors. Disrupting this general adaptor–LIC interface impairs processive dynein function, supporting a direct motor-assembly role rather than a merely passive cargo tether. (hoogenraad2016bicaudaldfamily pages 5-7)
In the prevailing model, intramolecular CC3–CC1 contacts maintain a compact or looped autoinhibited state that masks the motor-binding region. Cargo engagement, phosphorylation, or experimentally removing the C-terminal region shifts BICD2 toward an open state that binds dynein/dynactin efficiently. An N-terminal BICD2 fragment binds and activates dynein more strongly than full-length BICD2, while cargo or membrane tethering enables productive motility in cells. (splinter2012bicd2dynactinand pages 1-2, gallisasune2023bicd2phosphorylationregulates pages 1-2, zhao2024molecularmechanismfor pages 1-2, splinter2012bicd2dynactinand pages 10-12)
A compact mapping of modules, partners, and locations is provided below.
| Module/state | Binding partner or cargo | Cellular location | Mechanistic consequence | Strongest evidence/year |
|---|---|---|---|---|
| N-terminal CC1 | Cytoplasmic dynein, including light intermediate chain (LIC) | Cytosol and assembled cargo-associated dynein–dynactin complexes | Supplies the principal motor-binding interface; LIC binding and assembly with dynactin enable processive, microtubule-minus-end-directed transport | Biochemical interaction, reconstitution, and single-molecule motility studies, 2012–2019 (splinter2012bicd2dynactinand pages 1-2, hoogenraad2016bicaudaldfamily pages 4-5, hoogenraad2016bicaudaldfamily pages 5-7) |
| CC2 | Dynactin through the Spindly motif; kinesin-1 through a distinct central interaction region | Motor complexes on vesicular and nuclear cargoes | Stabilizes/activates dynein–dynactin while permitting coordination with an opposing plus-end-directed kinesin motor | Mechanistic review and biochemical/cellular evidence, 2016–2023 (gallisasune2023bicd2phosphorylationregulates pages 1-2, hoogenraad2016bicaudaldfamily pages 5-7, yi2023roleofnesprin2 pages 2-4) |
| C-terminal CC3/BICD cargo-binding region | Rab6-GTP, RanBP2/Nup358, Nesprin-2, and intramolecularly CC1 | Cargo membranes or nuclear envelope; folded toward CC1 in the cargo-free state | Selects cargo; CC3–CC1 interaction autoinhibits motor binding, whereas cargo engagement favors an open, dynein-activating conformation | Biochemical and structural/modeling evidence, 2016–2024 (gallisasune2023bicd2phosphorylationregulates pages 1-2, zhao2024molecularmechanismfor pages 1-2, gibson2023astructuralmodel pages 1-3) |
| Rab6-GTP-bound state | Active Rab6-GTP; dynein and kinesin-1 | Rab6-positive Golgi-derived and secretory vesicles, especially in G1/S and non-dividing cells | Links vesicles to a multimotor transport complex; interface-disrupting Rab6 mutations reduce BICD2 co-migration and strongly diminish vesicle motility | Structure prediction, mutagenesis, and live-cell transport assays, 2024 (zhao2024molecularmechanismfor pages 1-2) |
| RanBP2/Nup358-bound state | Phosphorylated RanBP2/Nup358; core interfaces at BICD2 residues 747–774 and 774–800 | Cytoplasmic face of the nuclear envelope/nuclear pore in G2 | Recruits dynein–dynactin to the nuclear envelope for nucleus–centrosome tethering, centrosome separation, and progenitor-cell nuclear positioning; overlaps the Rab6-binding region and thereby supports cargo switching | Modeling plus mutagenesis, 2023; cell-cycle experiments, 2023 (gallisasune2023bicd2phosphorylationregulates pages 1-2, gibson2023astructuralmodel pages 1-3) |
| Nesprin-2-bound state | Nesprin-2/LINC-complex machinery; dynein–dynactin and functionally coordinated kinesin-1 | Outer nuclear membrane of migrating post-mitotic neurons | Couples the nucleus to opposing microtubule motors, enabling persistent/bidirectional nuclear movement and neuronal migration; RanBP2 and Nesprin-2 binding are mutually exclusive | Biochemical competition and in-vivo brain assays, 2023; neuronal motor-coordination experiments, 2024 (yi2023roleofnesprin2 pages 7-9, yi2023roleofnesprin2 pages 1-2, zhou2024nesprin2coordinatesopposing pages 1-2) |
| CDK1–PLK1-activated state | CDK1, PLK1, dynein–dynactin, and phosphorylated RanBP2; PLK1 target Ser102 | Nuclear envelope and nucleus-associated centrosomes during G2/M | CDK1 primes PLK1 recruitment; PLK1 phosphorylation of Ser102 shifts BICD2 toward an active conformation, enhancing motor-complex assembly, nuclear-envelope recruitment, centrosome tethering, and separation | Phosphosite mapping, phosphomutants, interaction assays, and cellular phenotyping, 2023 (gallisasune2023bicd2phosphorylationregulates pages 2-3, gallisasune2023bicd2phosphorylationregulates pages 4-5, gallisasune2023bicd2phosphorylationregulates pages 5-6, gallisasune2023bicd2phosphorylationregulates pages 3-4) |
Table: This table maps human BICD2 structural modules and regulated cargo-bound states to their interaction partners, cellular locations, and mechanistic outcomes. It highlights the evidence supporting BICD2’s role as a cell-cycle- and cargo-regulated dynein–dynactin activating adaptor.
In G1/S and non-dividing cells, a major BICD2 pathway begins with GTP-bound Rab6 on Golgi-derived and secretory vesicles. The BICD2 C terminus binds Rab6-GTP and recruits both dynein and kinesin-1, creating a multimotor complex capable of regulated bidirectional trafficking. Relevant locations include the Golgi, cytoplasmic secretory carriers, and exocytic hotspots. (hoogenraad2016bicaudaldfamily pages 2-4, zhao2024molecularmechanismfor pages 1-2, gallisasune2023bicd2phosphorylationregulates pages 1-2)
A 2024 structural-modeling and mutagenesis study found that BICD2 recognizes two Rab6 regions that change conformation during GDP-to-GTP exchange. Reorganization of hydrophobic residues explains preferential recognition of active Rab6-GTP. Interface-disrupting Rab6 mutations reduced Rab6–BICD2 co-migration and severely diminished Rab6-positive-vesicle motility, establishing functional specificity in cells rather than binding alone. Published 7 May 2024, Life Science Alliance, DOI/URL: https://doi.org/10.26508/lsa.202302430. (zhao2024molecularmechanismfor pages 1-2)
In early G2, BICD2 changes localization from Rab6 membranes to the cytoplasmic face of nuclear pores, where it binds RanBP2/Nup358 and recruits dynein/dynactin. This pool links the nuclear envelope to microtubules, maintains nucleus–centrosome coupling, contributes to centrosome separation and mitotic-spindle organization, and drives apical interkinetic nuclear migration in radial glial progenitors. (hoogenraad2016bicaudaldfamily pages 2-4, gallisasune2023bicd2phosphorylationregulates pages 1-2)
The 2023 Nup358 structural study combined AlphaFold2, HADDOCK, ClusPro, and mutagenesis. It placed an induced Nup358 cargo-recognition helix antiparallel to BICD2 residues 747–774, identified two stabilizing intermolecular salt bridges, and proposed a second interface involving Nup358 disorder and BICD2 residues 774–800. The latter region overlaps the Rab6-binding area, giving a physical explanation for mutually competitive cargo selection. The reported complex has 2:2 stoichiometry. Published 26 September 2023, Biomolecules, DOI/URL: https://doi.org/10.3390/biom13101445. Because the atomic arrangement is modeling-led, its mutational support is important, but it should not be equated with an experimentally determined high-resolution complex structure. (gibson2023astructuralmodel pages 1-3)
In post-mitotic migrating neurons, BICD2 is recruited to the outer nuclear membrane by Nesprin-2, a LINC-complex component. This dynein–dynactin–BICD2 assembly moves and positions the nucleus during neuronal migration. RanBP2 and Nesprin-2 interactions are mutually exclusive, suggesting a developmental handoff: RanBP2–BICD2 drives progenitor interkinetic nuclear migration, whereas Nesprin-2–BICD2 supports migration after neuronal differentiation. (yi2023roleofnesprin2 pages 7-9, yi2023roleofnesprin2 pages 1-2)
In embryonic-rat-brain experiments, BICD2 depletion impaired both apical progenitor nuclear migration and neuronal migration toward the cortical plate. Cargo-selective patient variants separated these functions: E770G increased Nesprin-2 binding approximately sixfold while strongly reducing RanBP2 binding and failed to rescue progenitor nuclear migration; K785M nearly abolished both interactions. R690C retained sufficient RanBP2-pathway activity to restore nuclei to the ventricular region, operationally measured within 10 μm of the ventricular surface. Published March 2023, PLOS Genetics, DOI/URL: https://doi.org/10.1371/journal.pgen.1010642. (yi2023roleofnesprin2 pages 2-4, yi2023roleofnesprin2 pages 7-9)
A 2024 neuronal study further showed that Nesprin-2 coordinates dynein–dynactin–BicD2 and kinesin-1 rather than using them simply as antagonists. Disabling either motor-binding system impaired nuclear movement, supporting a model in which coordinated opposite-polarity motors produce persistent and bidirectional movement along advancing perinuclear microtubules. This evidence comes from mouse cerebellar granule neurons and therefore supports a conserved mammalian mechanism rather than being direct human-cell evidence. Published August 2024, Journal of Cell Biology, DOI/URL: https://doi.org/10.1083/jcb.202405032. (zhou2024nesprin2coordinatesopposing pages 1-2)
The strongest recent regulatory advance is a sequential CDK1–PLK1 phosphorylation circuit. During G2, CDK1 phosphorylation creates or strengthens a PLK1-docking state on BICD2; PLK1 then phosphorylates the BICD2 N terminus, particularly Ser102. Ser102 phosphorylation changes N–C-terminal interactions, shifts BICD2 toward an active conformation, facilitates dynein/dynactin assembly, and favors binding to phosphorylated RanBP2. Functionally, this pathway is required for nuclear-envelope dynein recruitment, nucleus–centrosome tethering, and timely centrosome separation. (gallisasune2023bicd2phosphorylationregulates pages 1-2, gallisasune2023bicd2phosphorylationregulates pages 2-3, gallisasune2023bicd2phosphorylationregulates pages 3-4)
Mass spectrometry also found PLK1 sites Thr289 and an unresolved Thr531/Ser533 site, while CDK1 assays identified Ser331 and an additional unresolved site among Thr319/Ser320/Thr321. Ser102 was the dominant PLK1 target in the 1–271 fragment and the clearest functionally analyzed activating site. In mitochondrial-clustering assays, full-length phosphomimetic S102D yielded clustering in 61% of cells versus 43% for nonphosphorylatable S102A and approximately 50% for wild type; an open BICD2 1–575 fragment produced approximately 85% clustering. Wild-type and S102D proteins remained similarly dimeric, approximately 190 kDa with an approximately 8-nm hydrodynamic radius, arguing against gross oligomeric disruption. Published April 2023, Nature Communications 14:2434, DOI/URL: https://doi.org/10.1038/s41467-023-38116-1. (gallisasune2023bicd2phosphorylationregulates pages 4-5, gallisasune2023bicd2phosphorylationregulates pages 5-6, gallisasune2023bicd2phosphorylationregulates pages 3-4)
Heterozygous pathogenic BICD2 variants cause spinal muscular atrophy with lower-extremity predominance type 2 (SMALED2) and related dominant congenital/proximal SMA or distal hereditary motor-neuron phenotypes. Typical disease features are early lower-limb-predominant weakness and muscle wasting, often relatively stable or slowly progressive, although severe prenatal presentations with contractures, arthrogryposis, and respiratory compromise occur. Open Targets integrates five evidence records for several BICD2-associated entities, including prenatal-onset SMALED2B and childhood-onset proximal SMA with contractures. (OpenTargets Search: -BICD2, hoogenraad2016bicaudaldfamily pages 9-10)
Mechanistically, BICD2 disease is not a single simple loss-of-function syndrome. At least 22 disease-associated mutations were catalogued in the 2023 brain-development study. Variants can affect motor-complex activation, autoinhibition, Rab6 secretion, kinesin coordination, or selective binding to RanBP2 and Nesprin-2. For example, S107L has been interpreted as increasing dynein–dynactin association, whereas a Q774-region substitution can reduce Rab6 interaction; patient fibroblasts have shown impaired Rab6A-dependent secretion. Thus, variant-specific gain of function, dominant-negative effects, altered cargo competition, and partial loss of function probably coexist. (yi2023roleofnesprin2 pages 2-4, hoogenraad2016bicaudaldfamily pages 9-10)
Some variants cause cortical-developmental abnormalities in addition to—or instead of—classic lower-motor-neuron disease. Experimental evidence directly links these phenotypes to failure of RanBP2- or Nesprin-2-dependent nuclear migration. The critical inference is that disease severity and tissue selectivity may depend less on total BICD2 abundance than on which cargo interface or conformational equilibrium is perturbed. (yi2023roleofnesprin2 pages 7-9, yi2023roleofnesprin2 pages 1-2, gibson2023astructuralmodel pages 1-3)
In a 2024 French cohort of 24 patients representing 23 families with non-5q proximal SMA, a causative diagnosis was obtained in 9/23 families (39%). Gene panels identified five DYNC1H1 and three BICD2 variants; exome sequencing after a negative panel did not identify a cause in 14 cases. The authors consequently favored targeted next-generation sequencing panels as the initial test, with trio exome or genome sequencing as second-line approaches. Published in European Journal of Human Genetics in 2024, DOI/URL: https://doi.org/10.1038/s41431-023-01407-8. These figures apply to this selected referral cohort, not population prevalence. (OpenTargets Search: -BICD2)
BICD2’s cargo-binding and dynein-activating functions are exploited by pathogens. A peer-reviewed 2024 study showed that HPV16 L2 capsid protein directly binds BICD2, recruiting dynein for transport along the endosome–TGN/Golgi route. Disabling BICD2 caused viral accumulation in endosomes and the TGN and inhibited infection; a short L2 C-terminal segment mediated direct binding. This identifies the L2–BICD2 interface as a potential antiviral intervention point, although no clinical inhibitor has yet been established. Published 3 June 2024, PLOS Pathogens 20:e1012289, DOI/URL: https://doi.org/10.1371/journal.ppat.1012289. (speckhart2024thebicd2dynein pages 24-25, speckhart2024thebicd2dynein pages 1-2)
HIV-1 has also been reported to engage dynein–dynactin–BICD2 during infection and nuclear transport, but that key primary report dates to 2018 rather than 2023–2024. DOI/URL: https://doi.org/10.1128/JVI.00358-18. (speckhart2024thebicd2dynein pages 25-25)
A 2024 bioRxiv preprint, not peer reviewed at posting, reported that Orientia tsutsugamushi ScaC recruits BICD1/2 to the bacterial surface. ScaC was sufficient to engage dynein, promoted opening of BICD2 in biochemical/single-molecule assays, and BICD2 was required for efficient perinuclear bacterial movement. Posted 25 April 2024, DOI/URL: https://doi.org/10.1101/2024.04.11.589026. This is mechanistically compelling but remains lower-certainty than the peer-reviewed HPV study. (manigrasso2024theintracellularbacterium pages 1-2)
Current real-world applications are therefore chiefly diagnostic and experimental: inclusion of BICD2 on hereditary motor-neuropathy/non-5q SMA sequencing panels; interpretation of variants by cargo-specific biochemical assays; use of BICD2 fragments to reconstitute or manipulate dynein transport; and investigation of pathogen–adaptor interfaces as antiviral or antibacterial targets. Broad therapeutic activation or inhibition of BICD2 would likely be risky because the same adaptor participates in secretion, nuclear positioning, mitosis, and neuronal development. A more plausible strategy is variant-, cargo-, or interface-selective modulation. (OpenTargets Search: -BICD2, zhao2024molecularmechanismfor pages 1-2, speckhart2024thebicd2dynein pages 1-2)
The most secure annotation is that BICD2 is a regulated dynein–dynactin activating adaptor with a separable motor-binding N terminus and cargo-selective C terminus. This conclusion is supported by purified-protein reconstitution, co-immunoprecipitation, live-cell cargo relocation, single-molecule motility, mutagenesis, phosphosite mapping, and in-vivo brain perturbation. (splinter2012bicd2dynactinand pages 1-2, hoogenraad2016bicaudaldfamily pages 5-7, yi2023roleofnesprin2 pages 7-9, gallisasune2023bicd2phosphorylationregulates pages 1-2)
The autoinhibition/opening model is also well supported, but full-length BICD2 is conformationally flexible, so individual compact structural models should be treated as ensembles rather than a single invariant state. Likewise, the 2023 Nup358 and 2024 Rab6 interface models are strengthened by mutagenesis and cell phenotypes but remain less definitive than high-resolution experimental structures of complete cargo-bound human BICD2 complexes. (fagiewicz2022invitrocharacterization pages 1-4, zhao2024molecularmechanismfor pages 1-2, gibson2023astructuralmodel pages 1-3)
The largest unresolved question is why different BICD2 variants selectively injure lower motor neurons or developing brain. Existing evidence favors altered cargo choice, motor balance, and activation state over a universal deficiency in dynein binding. Long axons, high secretory demand, and tightly regulated nucleokinesis may make neural cells especially sensitive, but these explanations remain mechanistic hypotheses rather than settled facts. (yi2023roleofnesprin2 pages 2-4, hoogenraad2016bicaudaldfamily pages 9-10)
Human BICD2/Q8TD16 is best functionally annotated as an intracellular, coiled-coil cargo adaptor and activator of cytoplasmic dynein-1–dynactin. It carries out this role principally on Rab6-positive Golgi/secretory vesicles and at the cytoplasmic nuclear envelope through RanBP2/Nup358 or Nesprin-2. Cargo binding and CDK1–PLK1 phosphorylation relieve autoinhibition, allowing assembly of processive motor complexes that control vesicle trafficking, nuclear positioning, centrosome behavior, and neuronal migration. Recent 2023–2024 studies have moved the field from a general adaptor model toward residue-level cargo recognition and phosphorylation-controlled activation, while human genetics shows that different molecular lesions produce distinct motor-neuron and neurodevelopmental outcomes. (gallisasune2023bicd2phosphorylationregulates pages 1-2, zhao2024molecularmechanismfor pages 1-2, gibson2023astructuralmodel pages 1-3)
References
(splinter2012bicd2dynactinand pages 1-2): Daniël Splinter, David S. Razafsky, Max A. Schlager, Andrea Serra-Marques, Ilya Grigoriev, Jeroen Demmers, Nanda Keijzer, Kai Jiang, Ina Poser, Anthony A. Hyman, Casper C. Hoogenraad, Stephen J. King, and Anna Akhmanova. Bicd2, dynactin, and lis1 cooperate in regulating dynein recruitment to cellular structures. Molecular Biology of the Cell, 23:4226-4241, Nov 2012. URL: https://doi.org/10.1091/mbc.e12-03-0210, doi:10.1091/mbc.e12-03-0210. This article has 318 citations and is from a domain leading peer-reviewed journal.
(hoogenraad2016bicaudaldfamily pages 5-7): Casper C. Hoogenraad and Anna Akhmanova. Bicaudal d family of motor adaptors: linking dynein motility to cargo binding. Trends in cell biology, 26 5:327-340, May 2016. URL: https://doi.org/10.1016/j.tcb.2016.01.001, doi:10.1016/j.tcb.2016.01.001. This article has 135 citations and is from a domain leading peer-reviewed journal.
(zhao2024molecularmechanismfor pages 1-2): Xiaoxin Zhao, Sebastian Quintremil, Estrella D Rodriguez Castro, Heying Cui, David Moraga, Tingyao Wang, Richard B Vallee, and Sozanne R Solmaz. Molecular mechanism for recognition of the cargo adapter rab6gtp by the dynein adapter bicd2. Life Science Alliance, 7:e202302430, May 2024. URL: https://doi.org/10.26508/lsa.202302430, doi:10.26508/lsa.202302430. This article has 8 citations and is from a peer-reviewed journal.
(yi2023roleofnesprin2 pages 2-4): Julie Yi, Xiaoxin Zhao, Crystal R. Noell, Paige Helmer, Sozanne R. Solmaz, and Richard B. Vallee. Role of nesprin-2 and ranbp2 in bicd2-associated brain developmental disorders. PLOS Genetics, 19:e1010642, Mar 2023. URL: https://doi.org/10.1371/journal.pgen.1010642, doi:10.1371/journal.pgen.1010642. This article has 20 citations and is from a domain leading peer-reviewed journal.
(gallisasune2023bicd2phosphorylationregulates pages 1-2): Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, and Joan Roig. Bicd2 phosphorylation regulates dynein function and centrosome separation in g2 and m. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38116-1, doi:10.1038/s41467-023-38116-1. This article has 25 citations and is from a highest quality peer-reviewed journal.
(gibson2023astructuralmodel pages 1-3): James M. Gibson, Xiaoxin Zhao, M. Yusuf Ali, Sozanne R. Solmaz, and Chunyu Wang. A structural model for the core nup358-bicd2 interface. Biomolecules, 13:1445, Sep 2023. URL: https://doi.org/10.3390/biom13101445, doi:10.3390/biom13101445. This article has 6 citations.
(fagiewicz2022invitrocharacterization pages 1-4): Robert Fagiewicz, Corinne Crucifix, Torben Klos, Célia Deville, Bruno Kieffer, Yves Nominé, Johan Busselez, Paola Rossolillo, and Helgo Schmidt. In vitro characterization of the full-length human dynein-1 cargo adaptor bicd2. bioRxiv, Jan 2022. URL: https://doi.org/10.1101/2022.01.05.474964, doi:10.1101/2022.01.05.474964. This article has 11 citations.
(OpenTargets Search: -BICD2): Open Targets Query (-BICD2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(gallisasune2023bicd2phosphorylationregulates pages 4-5): Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, and Joan Roig. Bicd2 phosphorylation regulates dynein function and centrosome separation in g2 and m. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38116-1, doi:10.1038/s41467-023-38116-1. This article has 25 citations and is from a highest quality peer-reviewed journal.
(hoogenraad2016bicaudaldfamily pages 4-5): Casper C. Hoogenraad and Anna Akhmanova. Bicaudal d family of motor adaptors: linking dynein motility to cargo binding. Trends in cell biology, 26 5:327-340, May 2016. URL: https://doi.org/10.1016/j.tcb.2016.01.001, doi:10.1016/j.tcb.2016.01.001. This article has 135 citations and is from a domain leading peer-reviewed journal.
(splinter2012bicd2dynactinand pages 10-12): Daniël Splinter, David S. Razafsky, Max A. Schlager, Andrea Serra-Marques, Ilya Grigoriev, Jeroen Demmers, Nanda Keijzer, Kai Jiang, Ina Poser, Anthony A. Hyman, Casper C. Hoogenraad, Stephen J. King, and Anna Akhmanova. Bicd2, dynactin, and lis1 cooperate in regulating dynein recruitment to cellular structures. Molecular Biology of the Cell, 23:4226-4241, Nov 2012. URL: https://doi.org/10.1091/mbc.e12-03-0210, doi:10.1091/mbc.e12-03-0210. This article has 318 citations and is from a domain leading peer-reviewed journal.
(yi2023roleofnesprin2 pages 7-9): Julie Yi, Xiaoxin Zhao, Crystal R. Noell, Paige Helmer, Sozanne R. Solmaz, and Richard B. Vallee. Role of nesprin-2 and ranbp2 in bicd2-associated brain developmental disorders. PLOS Genetics, 19:e1010642, Mar 2023. URL: https://doi.org/10.1371/journal.pgen.1010642, doi:10.1371/journal.pgen.1010642. This article has 20 citations and is from a domain leading peer-reviewed journal.
(yi2023roleofnesprin2 pages 1-2): Julie Yi, Xiaoxin Zhao, Crystal R. Noell, Paige Helmer, Sozanne R. Solmaz, and Richard B. Vallee. Role of nesprin-2 and ranbp2 in bicd2-associated brain developmental disorders. PLOS Genetics, 19:e1010642, Mar 2023. URL: https://doi.org/10.1371/journal.pgen.1010642, doi:10.1371/journal.pgen.1010642. This article has 20 citations and is from a domain leading peer-reviewed journal.
(zhou2024nesprin2coordinatesopposing pages 1-2): Chuying Zhou, You Kure Wu, Fumiyoshi Ishidate, Takahiro K. Fujiwara, and Mineko Kengaku. Nesprin-2 coordinates opposing microtubule motors during nuclear migration in neurons. The Journal of Cell Biology, Aug 2024. URL: https://doi.org/10.1083/jcb.202405032, doi:10.1083/jcb.202405032. This article has 25 citations.
(gallisasune2023bicd2phosphorylationregulates pages 2-3): Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, and Joan Roig. Bicd2 phosphorylation regulates dynein function and centrosome separation in g2 and m. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38116-1, doi:10.1038/s41467-023-38116-1. This article has 25 citations and is from a highest quality peer-reviewed journal.
(gallisasune2023bicd2phosphorylationregulates pages 5-6): Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, and Joan Roig. Bicd2 phosphorylation regulates dynein function and centrosome separation in g2 and m. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38116-1, doi:10.1038/s41467-023-38116-1. This article has 25 citations and is from a highest quality peer-reviewed journal.
(gallisasune2023bicd2phosphorylationregulates pages 3-4): Núria Gallisà-Suñé, Paula Sànchez-Fernàndez-de-Landa, Fabian Zimmermann, Marina Serna, Laura Regué, Joel Paz, Oscar Llorca, Jens Lüders, and Joan Roig. Bicd2 phosphorylation regulates dynein function and centrosome separation in g2 and m. Nature Communications, Apr 2023. URL: https://doi.org/10.1038/s41467-023-38116-1, doi:10.1038/s41467-023-38116-1. This article has 25 citations and is from a highest quality peer-reviewed journal.
(hoogenraad2016bicaudaldfamily pages 2-4): Casper C. Hoogenraad and Anna Akhmanova. Bicaudal d family of motor adaptors: linking dynein motility to cargo binding. Trends in cell biology, 26 5:327-340, May 2016. URL: https://doi.org/10.1016/j.tcb.2016.01.001, doi:10.1016/j.tcb.2016.01.001. This article has 135 citations and is from a domain leading peer-reviewed journal.
(hoogenraad2016bicaudaldfamily pages 9-10): Casper C. Hoogenraad and Anna Akhmanova. Bicaudal d family of motor adaptors: linking dynein motility to cargo binding. Trends in cell biology, 26 5:327-340, May 2016. URL: https://doi.org/10.1016/j.tcb.2016.01.001, doi:10.1016/j.tcb.2016.01.001. This article has 135 citations and is from a domain leading peer-reviewed journal.
(speckhart2024thebicd2dynein pages 24-25): Kaitlyn Speckhart, Jeongjoon Choi, Daniel DiMaio, and Billy Tsai. The bicd2 dynein cargo adaptor binds to the hpv16 l2 capsid protein and promotes hpv infection. Jun 2024. URL: https://doi.org/10.1371/journal.ppat.1012289, doi:10.1371/journal.ppat.1012289. This article has 11 citations and is from a highest quality peer-reviewed journal.
(speckhart2024thebicd2dynein pages 1-2): Kaitlyn Speckhart, Jeongjoon Choi, Daniel DiMaio, and Billy Tsai. The bicd2 dynein cargo adaptor binds to the hpv16 l2 capsid protein and promotes hpv infection. Jun 2024. URL: https://doi.org/10.1371/journal.ppat.1012289, doi:10.1371/journal.ppat.1012289. This article has 11 citations and is from a highest quality peer-reviewed journal.
(speckhart2024thebicd2dynein pages 25-25): Kaitlyn Speckhart, Jeongjoon Choi, Daniel DiMaio, and Billy Tsai. The bicd2 dynein cargo adaptor binds to the hpv16 l2 capsid protein and promotes hpv infection. Jun 2024. URL: https://doi.org/10.1371/journal.ppat.1012289, doi:10.1371/journal.ppat.1012289. This article has 11 citations and is from a highest quality peer-reviewed journal.
(manigrasso2024theintracellularbacterium pages 1-2): Giulia Manigrasso, Kittirat Saharat, Chitrasak Kullapanich, Jerome Boulanger, Tomos E. Morgan, Holger Kramer, Jeanne Salje, and Andrew P. Carter. The intracellular bacterium orientia tsutsugamushi hijacks the adaptor protein bicd2 for dynein-based motility. bioRxiv, Apr 2024. URL: https://doi.org/10.1101/2024.04.11.589026, doi:10.1101/2024.04.11.589026. This article has 6 citations.