DYNLRB2 encodes a subunit of the cytoplasmic dynein complex, a molecular motor responsible for retrograde microtubule-based transport . It is specifically upregulated in testicular tissue and linked to reproductive biology, viral infection mechanisms, and ciliopathies . Mutations or dysregulation of DYNLRB2 are associated with autosomal recessive deafness (DFNB77) and Bardet-Biedl syndrome .
DYNLRB2 is essential for bipolar spindle assembly during spermatocyte meiosis :
Meiotic Specificity: Exclusively expressed in meiotic spermatocytes, unlike its mitotic paralog DYNLRB1 .
Spindle Pole Integrity: Prevents fragmentation of pericentriolar material (PCM) by targeting NuMA (nuclear mitotic apparatus protein) to spindle poles .
KO Phenotype: Dynlrb2 knockout mice exhibit metaphase I arrest, multipolar spindles, and male infertility .
DYNLRB2 facilitates retrograde transport of murine leukemia virus (MLV) preintegration complexes (PICs) :
Nuclear Entry: Knockdown reduces PIC nuclear localization by 60% and decreases net transport speed by ~0.2 μm/s .
Motor Activity: Forms dynein complexes with comparable motility to DYNLRB1-containing complexes (~0.8 μm/s in vitro) .
TGF-β/Smad3 Signaling: Specifically regulates Smad3-mediated responses, unlike DYNLRB1, which influences Smad2 .
Ciliogenesis: Required for proper ciliary function; deficiencies correlate with hydrocephalus and defective spermiogenesis .
Interchangeable Roles: Ectopic DYNLRB2 rescues spindle defects in Dynlrb1-depleted mitotic cells, demonstrating functional overlap .
Paralog Comparison:
Dynein Light Chain Roadblock-Type 2 functions as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex . This complex acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules . The protein is thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function .
Recombinant Human DYNLRB2 protein is produced using Escherichia coli as the expression system . The protein is purified using anion-exchange chromatography and gel-filtration chromatography to achieve a purity of over 90% . This recombinant protein is suitable for various applications, including SDS-PAGE and mass spectrometry .