Results 1 to 10 of about 89 (74)
Comparative structural study on axonemal and cytoplasmic dyneins
AbstractAxonemal dyneins are the driving force of motile cilia, while cytoplasmic dyneins play an essential role in minus‐end oriented intracellular transport. Their molecular structure is indispensable for an understanding of the molecular mechanism of ciliary beating and cargo transport.
Takashi Ishikawa
exaly +5 more sources
Structure of a microtubule-bound axonemal dynein [PDF]
Abstract Axonemal dyneins are tethered to doublet microtubules inside cilia to drive ciliary beating, a process critical for cellular motility and extracellular fluid flow. Axonemal dyneins are evolutionarily and biochemically distinct from cytoplasmic dyneins that transport cargo, and the mechanisms regulating their localization and ...
Travis Walton, Hao Wu, Alan Brown
openaire +3 more sources
Cytoplasmic factories for axonemal dynein assembly [PDF]
ABSTRACT Axonemal dyneins power the beating of motile cilia and flagella. These massive multimeric motor complexes are assembled in the cytoplasm, and subsequently trafficked to cilia and incorporated into the axonemal superstructure. Numerous cytoplasmic factors are required for the dynein assembly process, and, in mammals, defects lead
openaire +2 more sources
Axonemal dyneins form the inner and outer rows of arms associated with the doublet microtubules of motile cilia. These enzymes convert the chemical energy released from adenosine triphosphate (ATP) hydrolysis into mechanical work by causing the doublets to slide with respect to each other.
openaire +2 more sources
The Motility of Axonemal Dynein is Regulated by the Tubulin Code [PDF]
Microtubule diversity, arising from the utilization of different tubulin genes and from posttranslational modifications, regulates many cellular processes including cell division, neuronal differentiation and growth, and centriole assembly. In the case of cilia and flagella, multiple cell biological studies show that microtubule diversity is important ...
Alper, J. +3 more
openaire +4 more sources
Ciliary Motility: Regulation of Axonemal Dynein Motors [PDF]
Ciliary motility is crucial for the development and health of many organisms. Motility depends on the coordinated activity of multiple dynein motors arranged in a precise pattern on the outer doublet microtubules. Although significant progress has been made in elucidating the composition and organization of the dyneins, a comprehensive understanding of
Rasagnya, Viswanadha +2 more
openaire +2 more sources
The Coordination and Regulation of Axonemal Dynein [PDF]
Molecular motor proteins drive the motility behind cellular dynamics. Recent advances in structural biology and single-molecule biophysics have led to a detailed understanding of many motor protein mechanisms. However, two understudied areas include the regulation and the coordination of motor proteins, particularly axonemal dyneins, which are the ...
openaire +1 more source
Torque Generation by Axonemal Outer-Arm Dynein [PDF]
Outer-arm dynein is the main engine providing the motive force in cilia. Using three-dimensional tracking microscopy, we found that contrary to previous reports Tetrahymena ciliary three-headed outer-arm dynein (αβγ) as well as proteolytically generated two-headed (βγ) and one-headed (α) subparticles showed clockwise rotation of each sliding ...
Yamaguchi, Shin +5 more
openaire +2 more sources
Functional Specialization of Respiratory and Olfactory Mucus Revealed by Proteomic Profiling
ABSTRACT Background Mucus overlies the nasal mucosa in the respiratory and olfactory regions, which perform distinct physiological functions. However, proteomic differences between respiratory mucosa (RM) and olfactory cleft (OC) mucus remain unclear.
Anna Kristina Hernandez +7 more
wiley +1 more source
ABSTRACT We here describe mouse models with complementary homozygous Svil mutations. In skeletal muscle, Svil‐Mut mice express the Svil‐encoded N‐terminus fused to the βgal‐neo gene‐trap tag and lack the highly conserved archvillin C‐terminus; Svil‐KO mice lack expression of all known Svil‐encoded proteins; and Svil‐LoxP mice contain loxP sites for ...
Tara C. Smith +9 more
wiley +1 more source

