Dynactin subunit 1 is a protein that in humans is encoded by the DCTN1 gene. [5]
This gene encodes the largest subunit of dynactin, a macromolecular complex consisting of 23 subunits (11 individual proteins ranging in size from 22 to 150 kD). [6] Dynactin binds to cytoplasmic dynein, dynein cargo adaptors, and microtubules. [7] It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis.
This subunit is commonly referred to p150-glued. [5] It is present in two copies per dynactin complex and forms an ≈75 nm long flexible arm that extends from the main body of dynactin. [6] The p150-glued arm contains binding sites for microtubules, [8] the microtubule plus tip binding protein EB1, [9] and the N-terminus of the dynein intermediate chain. [10] [11]
Alternative splicing of this gene results in at least 2 functionally distinct isoforms: a ubiquitously expressed one and a brain-specific one. Based on its cytogenetic location, this gene is considered as a candidate gene for limb-girdle muscular dystrophy. [12]
DCTN1 has been shown to interact with:
Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport.
Actin beta is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.
AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.
Tubulin beta-2A chain is a protein that in humans is encoded by the TUBB2A gene.
Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).
Tubulin alpha-4A chain is a protein that in humans is encoded by the TUBA4A gene.
Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene
Microtubule-associated protein RP/EB family member 1 is a protein that in humans is encoded by the MAPRE1 gene.
Alpha-centractin (yeast) or ARP1 is a protein that in humans is encoded by the ACTR1A gene.
Cytoplasmic dynein 1 intermediate chain 2 is a protein that in humans is encoded by the DYNC1I2 gene.
Dynein light chain Tctex-type 1 is a protein that in humans is encoded by the DYNLT1 gene.
Cytoplasmic dynein 1 intermediate chain 1 is a protein that in humans is encoded by the DYNC1I1 gene.
Spectrin beta chain, brain 2 is a protein that in humans is encoded by the SPTBN2 gene.
Dynactin subunit 3 is a protein that in humans is encoded by the DCTN3 gene.
Eukaryotic translation initiation factor 3 subunit K (eIF3k) is a protein that in humans is encoded by the EIF3K gene.
Tight junction protein ZO-3 is a protein that in humans is encoded by the TJP3 gene.
Phosphoinositide 3-kinase regulatory subunit 4, also known as PI3-kinase regulatory subunit 4 or PI3-kinase p150 subunit or phosphoinositide 3-kinase adaptor protein, or VPS15 is an enzyme that in humans is encoded by the PIK3R4 gene.
In molecular biology, DCTN6 is that subunit of the dynactin protein complex that is encoded by the p27 gene. Dynactin is the essential component for microtubule-based cytoplasmic dynein motor activity in intracellular transport of a variety of cargoes and organelles.
Dynactin subunit 4 is a protein that in humans is encoded by the DCTN4 gene.
Erika L F. Holzbaur is an American biologist who is the William Maul Measey Professor of Physiology at University of Pennsylvania Perelman School of Medicine. Her research considers the dynamics of organelle motility along cytoskeleton of cells. She is particularly interested in the molecular mechanisms that underpin neurodegenerative diseases.