Differential regulation of dynein-driven melanosome movement

Amy R. Reilein; Anna S. Serpinskaya; Ryan L. Karcher; Denis L. Dujardin; Richard B. Vallee; Vladimir I. Gelfand

doi:10.1016/j.bbrc.2003.08.047

Differential regulation of dynein-driven melanosome movement

Amy R. Reilein, Anna S. Serpinskaya, Ryan L. Karcher, Denis L. Dujardin, Richard B. Vallee, Vladimir I. Gelfand^*

^*Corresponding author for this work

Cell & Developmental Biology

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Cytoplasmic dyneins are multisubunit minus-end-directed microtubule motors. Different isoforms of dynein are thought to provide a means for independent movement of different organelles. We investigated the differential regulation of dynein-driven transport of pigment organelles (melanosomes) in Xenopus melanophores. Aggregation of melanosomes to the cell center does not change the localization of mitochondria, nor does dispersion of melanosomes cause a change in the perinuclear localization of the Golgi complex, indicating that melanosomes bear a dedicated form of dynein. We examined the subcellular fractionation behavior of dynein light intermediate chains (LIC) and identified at least three forms immunologically, only one of which fractionated with melanosomes. Melanosome aggregation was specifically blocked after injection of an antibody recognizing this LIC. Our data indicate that melanosome-associated dynein is regulated independently of bulk cytoplasmic dynein and involves a subfraction of dynein with a distinct subunit composition.

Original language	English (US)
Pages (from-to)	652-658
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	309
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2003.08.047
State	Published - Sep 26 2003

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Differential regulation of dynein-driven melanosome movement",

abstract = "Cytoplasmic dyneins are multisubunit minus-end-directed microtubule motors. Different isoforms of dynein are thought to provide a means for independent movement of different organelles. We investigated the differential regulation of dynein-driven transport of pigment organelles (melanosomes) in Xenopus melanophores. Aggregation of melanosomes to the cell center does not change the localization of mitochondria, nor does dispersion of melanosomes cause a change in the perinuclear localization of the Golgi complex, indicating that melanosomes bear a dedicated form of dynein. We examined the subcellular fractionation behavior of dynein light intermediate chains (LIC) and identified at least three forms immunologically, only one of which fractionated with melanosomes. Melanosome aggregation was specifically blocked after injection of an antibody recognizing this LIC. Our data indicate that melanosome-associated dynein is regulated independently of bulk cytoplasmic dynein and involves a subfraction of dynein with a distinct subunit composition.",

author = "Reilein, {Amy R.} and Serpinskaya, {Anna S.} and Karcher, {Ryan L.} and Dujardin, {Denis L.} and Vallee, {Richard B.} and Gelfand, {Vladimir I.}",

note = "Funding Information: We are grateful to Dr. Trina Schroer (Johns Hopkins University) for the antibody to DLC-A and to Dr. Viki Allan (University of Manchester, United Kingdom) for the antibody to Xenopus LICs. This work was supported by NIH grant GM 52111 to V.I.G.",

year = "2003",

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doi = "10.1016/j.bbrc.2003.08.047",

language = "English (US)",

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AU - Reilein, Amy R.

AU - Serpinskaya, Anna S.

AU - Karcher, Ryan L.

AU - Dujardin, Denis L.

AU - Vallee, Richard B.

AU - Gelfand, Vladimir I.

N1 - Funding Information: We are grateful to Dr. Trina Schroer (Johns Hopkins University) for the antibody to DLC-A and to Dr. Viki Allan (University of Manchester, United Kingdom) for the antibody to Xenopus LICs. This work was supported by NIH grant GM 52111 to V.I.G.

PY - 2003/9/26

Y1 - 2003/9/26

N2 - Cytoplasmic dyneins are multisubunit minus-end-directed microtubule motors. Different isoforms of dynein are thought to provide a means for independent movement of different organelles. We investigated the differential regulation of dynein-driven transport of pigment organelles (melanosomes) in Xenopus melanophores. Aggregation of melanosomes to the cell center does not change the localization of mitochondria, nor does dispersion of melanosomes cause a change in the perinuclear localization of the Golgi complex, indicating that melanosomes bear a dedicated form of dynein. We examined the subcellular fractionation behavior of dynein light intermediate chains (LIC) and identified at least three forms immunologically, only one of which fractionated with melanosomes. Melanosome aggregation was specifically blocked after injection of an antibody recognizing this LIC. Our data indicate that melanosome-associated dynein is regulated independently of bulk cytoplasmic dynein and involves a subfraction of dynein with a distinct subunit composition.

AB - Cytoplasmic dyneins are multisubunit minus-end-directed microtubule motors. Different isoforms of dynein are thought to provide a means for independent movement of different organelles. We investigated the differential regulation of dynein-driven transport of pigment organelles (melanosomes) in Xenopus melanophores. Aggregation of melanosomes to the cell center does not change the localization of mitochondria, nor does dispersion of melanosomes cause a change in the perinuclear localization of the Golgi complex, indicating that melanosomes bear a dedicated form of dynein. We examined the subcellular fractionation behavior of dynein light intermediate chains (LIC) and identified at least three forms immunologically, only one of which fractionated with melanosomes. Melanosome aggregation was specifically blocked after injection of an antibody recognizing this LIC. Our data indicate that melanosome-associated dynein is regulated independently of bulk cytoplasmic dynein and involves a subfraction of dynein with a distinct subunit composition.

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Differential regulation of dynein-driven melanosome movement

Abstract

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