Dynein Light Chain

Dynein Light Chain

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About Dynein Light Chain:

Dynein was first discovered and then named in 1963 by Ian R. Gibbons. It consists of various chains. These are heavy, intermediate, light intermediate and light. They are commonly divided into two different groups. These are cytoplasmic and axonemal dyneins. Cytoplasmic dynein is responsible for cell mitosis and intracellular transport and axonemal dynein is involved in ciliary/flagellar beating.
Dynein Light Chain (DNAL, DYNL) is encoded by the DYNLL1 gene in humans and is classed as a cytoplasmic protein.
The name dynein light chain itself is derived from the original description of DYNL in the dynein motor complex as a small molecular weight.

Dynein Light Chain Structure
The structure of DNAL/DYNL consists of:
1.Heavy - 530 kDA
2.Intermediate - 74 kDA
3.Light intermediate - 33-59 kDA
4.Light chain - 10-20 kDA

Dynein Light Chain Function
Dyneins have a molecular mass of approximately 1,200 kD. They are large enzyme complexes. DNAL/DYNL is heavily involved in intracellular motility and transport. The light chain exists as part of this and inhibits neuronal nitric oxide synthase activity.
Through its oxide synthase activity, it may be responsible for the regulation of various biological processes.

Dynein Light Chain Interactions
Since its discovery, DYNL has been observed to interact with the following:
●Bcl-2-like protein 11 (BCL2L1)
●PSD-95 (postsynaptic density protein 95) - (DLG4)
●Disks large-associated protein 1 - (DLGAP1)
●Cytoplasmic dynein 1 intermediate chain 1 - (DYNC1I1)
●nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha) -(IκBα)
●Myosin-Va - (MYO5A)
●Nuclear respiratory factor 1 - (NRF1)
●Serine/threonine-protein kinase - (PAK1)
●Tumour suppressor p53-binding protein 1 - (TP53BP1)