Characterization of the KLP68D kinesin-like protein in Drosophila

Possible roles in axonal transport

Patricia Pesavento, Russell J. Stewart, Lawrence S B Goldstein

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

This paper describes the molecular and biochemical properties of KLP68D, a new kinesin-like motor protein in Drosophila melanogaster. Sequence analysis of a full-length cDNA encoding KLP68D demonstrates that this protein has a domain that shares significant sequence identity with the entire 340-amin acid kinesin heavy chain motor domain. Sequences extending beyond the motor domain predict a region of alpha-helical coiled-coil followed by a globular 'tail' region; there is significant sequence similarity between the alpha- helical coiled-coil region of the KLP68D protein and similar regions of the KIF3 protein of mouse and the KRP85 protein of sea urchin. This finding suggests that all three proteins may be members of the same family, and that they all perform related functions. KLP68D protein produced in Escherichia coli is, like kinesin itself, a plus-end directed microtubule motor. In situ hybridization analysis of KLP68D RNA in Drosophila embryos indicates that the KLP68D gene is expressed primarily in the central nervous system and in a subset of the peripheral nervous system during embryogenesis. Thus, KLP68D may be used for anterograde axonal transport and could conceivably move cargoes in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.

Original languageEnglish (US)
Pages (from-to)1041-1048
Number of pages8
JournalJournal of Cell Biology
Volume127
Issue number4
DOIs
StatePublished - Nov 1994
Externally publishedYes

Fingerprint

Kinesin
Axonal Transport
Proteins
Drosophila Proteins
Sea Urchins
Peripheral Nervous System
Microtubules
Diptera
Drosophila
Embryonic Development
In Situ Hybridization
Sequence Analysis
Drosophila inturned protein
Tail
Embryonic Structures
Central Nervous System
Complementary DNA
RNA
Escherichia coli
Neurons

ASJC Scopus subject areas

  • Cell Biology

Cite this

Characterization of the KLP68D kinesin-like protein in Drosophila : Possible roles in axonal transport. / Pesavento, Patricia; Stewart, Russell J.; Goldstein, Lawrence S B.

In: Journal of Cell Biology, Vol. 127, No. 4, 11.1994, p. 1041-1048.

Research output: Contribution to journalArticle

Pesavento, Patricia ; Stewart, Russell J. ; Goldstein, Lawrence S B. / Characterization of the KLP68D kinesin-like protein in Drosophila : Possible roles in axonal transport. In: Journal of Cell Biology. 1994 ; Vol. 127, No. 4. pp. 1041-1048.
@article{3326c8a1424441e1be1b532190e4eba5,
title = "Characterization of the KLP68D kinesin-like protein in Drosophila: Possible roles in axonal transport",
abstract = "This paper describes the molecular and biochemical properties of KLP68D, a new kinesin-like motor protein in Drosophila melanogaster. Sequence analysis of a full-length cDNA encoding KLP68D demonstrates that this protein has a domain that shares significant sequence identity with the entire 340-amin acid kinesin heavy chain motor domain. Sequences extending beyond the motor domain predict a region of alpha-helical coiled-coil followed by a globular 'tail' region; there is significant sequence similarity between the alpha- helical coiled-coil region of the KLP68D protein and similar regions of the KIF3 protein of mouse and the KRP85 protein of sea urchin. This finding suggests that all three proteins may be members of the same family, and that they all perform related functions. KLP68D protein produced in Escherichia coli is, like kinesin itself, a plus-end directed microtubule motor. In situ hybridization analysis of KLP68D RNA in Drosophila embryos indicates that the KLP68D gene is expressed primarily in the central nervous system and in a subset of the peripheral nervous system during embryogenesis. Thus, KLP68D may be used for anterograde axonal transport and could conceivably move cargoes in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.",
author = "Patricia Pesavento and Stewart, {Russell J.} and Goldstein, {Lawrence S B}",
year = "1994",
month = "11",
doi = "10.1083/jcb.127.4.1041",
language = "English (US)",
volume = "127",
pages = "1041--1048",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

TY - JOUR

T1 - Characterization of the KLP68D kinesin-like protein in Drosophila

T2 - Possible roles in axonal transport

AU - Pesavento, Patricia

AU - Stewart, Russell J.

AU - Goldstein, Lawrence S B

PY - 1994/11

Y1 - 1994/11

N2 - This paper describes the molecular and biochemical properties of KLP68D, a new kinesin-like motor protein in Drosophila melanogaster. Sequence analysis of a full-length cDNA encoding KLP68D demonstrates that this protein has a domain that shares significant sequence identity with the entire 340-amin acid kinesin heavy chain motor domain. Sequences extending beyond the motor domain predict a region of alpha-helical coiled-coil followed by a globular 'tail' region; there is significant sequence similarity between the alpha- helical coiled-coil region of the KLP68D protein and similar regions of the KIF3 protein of mouse and the KRP85 protein of sea urchin. This finding suggests that all three proteins may be members of the same family, and that they all perform related functions. KLP68D protein produced in Escherichia coli is, like kinesin itself, a plus-end directed microtubule motor. In situ hybridization analysis of KLP68D RNA in Drosophila embryos indicates that the KLP68D gene is expressed primarily in the central nervous system and in a subset of the peripheral nervous system during embryogenesis. Thus, KLP68D may be used for anterograde axonal transport and could conceivably move cargoes in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.

AB - This paper describes the molecular and biochemical properties of KLP68D, a new kinesin-like motor protein in Drosophila melanogaster. Sequence analysis of a full-length cDNA encoding KLP68D demonstrates that this protein has a domain that shares significant sequence identity with the entire 340-amin acid kinesin heavy chain motor domain. Sequences extending beyond the motor domain predict a region of alpha-helical coiled-coil followed by a globular 'tail' region; there is significant sequence similarity between the alpha- helical coiled-coil region of the KLP68D protein and similar regions of the KIF3 protein of mouse and the KRP85 protein of sea urchin. This finding suggests that all three proteins may be members of the same family, and that they all perform related functions. KLP68D protein produced in Escherichia coli is, like kinesin itself, a plus-end directed microtubule motor. In situ hybridization analysis of KLP68D RNA in Drosophila embryos indicates that the KLP68D gene is expressed primarily in the central nervous system and in a subset of the peripheral nervous system during embryogenesis. Thus, KLP68D may be used for anterograde axonal transport and could conceivably move cargoes in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors.

UR - http://www.scopus.com/inward/record.url?scp=0028028334&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028028334&partnerID=8YFLogxK

U2 - 10.1083/jcb.127.4.1041

DO - 10.1083/jcb.127.4.1041

M3 - Article

VL - 127

SP - 1041

EP - 1048

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 4

ER -