DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond
The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are
highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein …
highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein …
[HTML][HTML] Sex differences in NSAID-induced perturbation of human intestinal barrier function and microbiota
S Edogawa, SA Peters, GD Jenkins… - The FASEB …, 2018 - ncbi.nlm.nih.gov
Intestinal barrier function and microbiota are integrally related and play critical roles in
maintenance of host physiology. Sex is a key biologic variable for several disorders. Our aim …
maintenance of host physiology. Sex is a key biologic variable for several disorders. Our aim …
[HTML][HTML] ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional transcriptional activator and feedback sensor in the regulation of dynein light chain …
S Jurado, LA Conlan, EK Baker, JL Ng, N Tenis… - Journal of Biological …, 2012 - ASBMB
The highly conserved DYNLL1 (LC8) protein was originally discovered as a light chain of
the dynein motor complex, but is increasingly emerging as a sequence-specific regulator of …
the dynein motor complex, but is increasingly emerging as a sequence-specific regulator of …
Dysregulated dynein-mediated trafficking of nephrin causes INF2-related podocytopathy
H Sun, C Perez-Gill, JS Schlöndorff… - Journal of the …, 2021 - journals.lww.com
Background FSGS caused by mutations in INF2 is characterized by a podocytopathy with
mistrafficked nephrin, an essential component of the slit diaphragm. Because INF2 is a …
mistrafficked nephrin, an essential component of the slit diaphragm. Because INF2 is a …
[HTML][HTML] Actin clearance promotes polarized dynein accumulation at the immunological synapse
Immunological synapse (IS) formation between a T cell and an antigen-presenting cell is
accompanied by the reorientation of the T cell centrosome toward the interface. This …
accompanied by the reorientation of the T cell centrosome toward the interface. This …
[HTML][HTML] Dynein and dynactin leverage their bivalent character to form a high-affinity interaction
Cytoplasmic dynein and dynactin participate in retrograde transport of organelles,
checkpoint signaling and cell division. The principal subunits that mediate this interaction …
checkpoint signaling and cell division. The principal subunits that mediate this interaction …
Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
MD Stuchell-Brereton, A Siglin, J Li… - Molecular biology of …, 2011 - Am Soc Cell Biol
Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the
positioning of various organelles. Dynein light chain (LC) subunits are conserved across …
positioning of various organelles. Dynein light chain (LC) subunits are conserved across …
GPCR kinase 2–interacting protein‐1 protects against ischemia‐reperfusion injury of the spinal cord by modulating ASK1/JNK/p38 signaling
ABSTRACT GPCR kinase 2–interacting protein‐1 (GIT1) is a scaffold protein that plays an
important role in cell adaptation, proliferation, migration, and differentiation; however, the …
important role in cell adaptation, proliferation, migration, and differentiation; however, the …
[HTML][HTML] Dynein light chain 1 (LC8) association enhances microtubule stability and promotes microtubule bundling
Dynein light chain 1 (LC8), a highly conserved protein, is known to bind to a variety of
different polypeptides. It functions as a dimer, which is inactivated through phosphorylation …
different polypeptides. It functions as a dimer, which is inactivated through phosphorylation …
[HTML][HTML] Affinity, avidity, and kinetics of target sequence binding to LC8 dynein light chain isoforms
LC8 dynein light chain (DYNLL) is a highly conserved eukaryotic hub protein with dozens of
binding partners and various functions beyond being a subunit of dynein and myosin Va …
binding partners and various functions beyond being a subunit of dynein and myosin Va …