The auto-inhibitory domain and ATP-independent microtubule-binding region of Kinesin heavy chain are major functional domains for transport in the Drosophila germline
| Autor: | Bing Fu Ng, Philippe Loiseau, Sujoy Ganguly, Lucy S. Williams, Isabel M. Palacios |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Body plan
Dynein Kinesins Plasma protein binding macromolecular substances Inhibitory postsynaptic potential Motor proteins Microtubules Germline Domain (software engineering) Motor protein Animals Genetically Modified 03 medical and health sciences Cell asymmetries 0302 clinical medicine Oogenesis Microtubule Animals Drosophila Proteins RNA Messenger Kinesin 8 Drosophila (subgenus) Molecular Biology Research Articles Cytoskeleton 030304 developmental biology Kinesin Heavy Chain Genetics 0303 health sciences Binding Sites biology Cell Polarity Dyneins Cell Biology Transforming Growth Factor alpha biology.organism_classification Transport protein Cell biology Protein Structure Tertiary Protein Transport Drosophila melanogaster Kinesin Intracellular transport Drosophila Protein 030217 neurology & neurosurgery Developmental Biology Protein Binding |
| Zdroj: | Development (Cambridge, England) |
| ISSN: | 1477-9129 0950-1991 |
| Popis: | The major motor Kinesin-1 provides a key pathway for cell polarization through intracellular transport. Little is known about how Kinesin works in complex cellular surroundings. Several cargos associate with Kinesin via Kinesin light chain (KLC). However, KLC is not required for all Kinesin transport. A putative cargo-binding domain was identified in the C-terminal tail of fungal Kinesin heavy chain (KHC). The tail is conserved in animal KHCs and might therefore represent an alternative KLC-independent cargo-interacting region. By comprehensive functional analysis of the tail during Drosophila oogenesis we have gained an understanding of how KHC achieves specificity in its transport and how it is regulated. This is, to our knowledge, the first in vivo structural/functional analysis of the tail in animal Kinesins. We show that the tail is essential for all functions of KHC except Dynein transport, which is KLC dependent. These tail-dependent KHC activities can be functionally separated from one another by further characterizing domains within the tail. In particular, our data show the following. First, KHC is temporally regulated during oogenesis. Second, the IAK domain has an essential role distinct from its auto-inhibitory function. Third, lack of auto-inhibition in itself is not necessarily detrimental to KHC function. Finally, the ATP-independent microtubule-binding motif is required for cargo localization. These results stress that two unexpected highly conserved domains, namely the auto-inhibitory IAK and the auxiliary microtubule-binding motifs, are crucial for transport by Kinesin-1 and that, although not all cargos are conserved, their transport involves the most conserved domains of animal KHCs. |
| Databáze: | OpenAIRE |
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