Microtubule-based transport along axons, dendrites and axonemes

Dawn Signor, Jonathan M. Scholey

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

• MTs in cytoplasmic extensions including axons, dendrites and axonemes serve as polarized tracks for vectorial intracellular transport driven by MT-based motor proteins. • Although axons and axonemes serve very different functions, increasing evidence suggests that the transport events, MT organization and the motors involved in their formation and function are conserved. Thus, there are obvious similarities in the mechanisms of axonal transport and IFT. • The MT arrays of axons and axonemes are parallel, whereas those of dendrites are anti-parallel, but the functional significance of this difference and its consequences for mechanisms of transport along these processes are unclear. • MT-based motor proteins of the dynein and kinesin superfamilies transport a variety of cargos including membrane-bound vesicles and macromolecular complexes along MTs of axons, dendrites and axonemes, and thus contribute to the formation, maintenance and function of these cytoplasmic extensions. • Chemosensory neurons in the nematode C. elegans represent an appealing system for studying transport events along dendrites and axonemes that occur sequentially in a single cell.

Original languageEnglish (US)
Pages (from-to)89-102
Number of pages14
JournalEssays in Biochemistry
Volume35
StatePublished - 2000

Fingerprint

Axoneme
Dendrites
Microtubules
Axons
Macromolecular Substances
Dyneins
Kinesin
Axonal Transport
Neurons
Proteins
Membranes
Maintenance

ASJC Scopus subject areas

  • Biochemistry

Cite this

Microtubule-based transport along axons, dendrites and axonemes. / Signor, Dawn; Scholey, Jonathan M.

In: Essays in Biochemistry, Vol. 35, 2000, p. 89-102.

Research output: Contribution to journalArticle

Signor, Dawn ; Scholey, Jonathan M. / Microtubule-based transport along axons, dendrites and axonemes. In: Essays in Biochemistry. 2000 ; Vol. 35. pp. 89-102.
@article{1733963b1d504d94ad07415372dcf4a4,
title = "Microtubule-based transport along axons, dendrites and axonemes",
abstract = "• MTs in cytoplasmic extensions including axons, dendrites and axonemes serve as polarized tracks for vectorial intracellular transport driven by MT-based motor proteins. • Although axons and axonemes serve very different functions, increasing evidence suggests that the transport events, MT organization and the motors involved in their formation and function are conserved. Thus, there are obvious similarities in the mechanisms of axonal transport and IFT. • The MT arrays of axons and axonemes are parallel, whereas those of dendrites are anti-parallel, but the functional significance of this difference and its consequences for mechanisms of transport along these processes are unclear. • MT-based motor proteins of the dynein and kinesin superfamilies transport a variety of cargos including membrane-bound vesicles and macromolecular complexes along MTs of axons, dendrites and axonemes, and thus contribute to the formation, maintenance and function of these cytoplasmic extensions. • Chemosensory neurons in the nematode C. elegans represent an appealing system for studying transport events along dendrites and axonemes that occur sequentially in a single cell.",
author = "Dawn Signor and Scholey, {Jonathan M.}",
year = "2000",
language = "English (US)",
volume = "35",
pages = "89--102",
journal = "Essays in Biochemistry",
issn = "0071-1365",
publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Microtubule-based transport along axons, dendrites and axonemes

AU - Signor, Dawn

AU - Scholey, Jonathan M.

PY - 2000

Y1 - 2000

N2 - • MTs in cytoplasmic extensions including axons, dendrites and axonemes serve as polarized tracks for vectorial intracellular transport driven by MT-based motor proteins. • Although axons and axonemes serve very different functions, increasing evidence suggests that the transport events, MT organization and the motors involved in their formation and function are conserved. Thus, there are obvious similarities in the mechanisms of axonal transport and IFT. • The MT arrays of axons and axonemes are parallel, whereas those of dendrites are anti-parallel, but the functional significance of this difference and its consequences for mechanisms of transport along these processes are unclear. • MT-based motor proteins of the dynein and kinesin superfamilies transport a variety of cargos including membrane-bound vesicles and macromolecular complexes along MTs of axons, dendrites and axonemes, and thus contribute to the formation, maintenance and function of these cytoplasmic extensions. • Chemosensory neurons in the nematode C. elegans represent an appealing system for studying transport events along dendrites and axonemes that occur sequentially in a single cell.

AB - • MTs in cytoplasmic extensions including axons, dendrites and axonemes serve as polarized tracks for vectorial intracellular transport driven by MT-based motor proteins. • Although axons and axonemes serve very different functions, increasing evidence suggests that the transport events, MT organization and the motors involved in their formation and function are conserved. Thus, there are obvious similarities in the mechanisms of axonal transport and IFT. • The MT arrays of axons and axonemes are parallel, whereas those of dendrites are anti-parallel, but the functional significance of this difference and its consequences for mechanisms of transport along these processes are unclear. • MT-based motor proteins of the dynein and kinesin superfamilies transport a variety of cargos including membrane-bound vesicles and macromolecular complexes along MTs of axons, dendrites and axonemes, and thus contribute to the formation, maintenance and function of these cytoplasmic extensions. • Chemosensory neurons in the nematode C. elegans represent an appealing system for studying transport events along dendrites and axonemes that occur sequentially in a single cell.

UR - http://www.scopus.com/inward/record.url?scp=0034351413&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034351413&partnerID=8YFLogxK

M3 - Article

C2 - 12471892

AN - SCOPUS:0034351413

VL - 35

SP - 89

EP - 102

JO - Essays in Biochemistry

JF - Essays in Biochemistry

SN - 0071-1365

ER -