Regulation of Phospholipase D Activity by Actin: ACTIN EXERTS BIDIRECTIONAL MODULATION OF MAMMALIAN PHOSPOLIPASE D ACTIVITY IN A POLYMERIZATION-DEPENDENT, ISOFORM-SPECIFIC MANNER

David J Kusner; James A Barton; Kuo-Kuang Wen; Xuemin Wang; Peter A Rubenstein; Shankar S Iyer

doi:10.1074/jbc.M209221200

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Regulation of Phospholipase D Activity by Actin: ACTIN EXERTS BIDIRECTIONAL MODULATION OF MAMMALIAN PHOSPOLIPASE D ACTIVITY IN A POLYMERIZATION-DEPENDENT, ISOFORM-SPECIFIC MANNER

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Regulation of Phospholipase D Activity by Actin: ACTIN EXERTS BIDIRECTIONAL MODULATION OF MAMMALIAN PHOSPOLIPASE D ACTIVITY IN A POLYMERIZATION-DEPENDENT, ISOFORM-SPECIFIC MANNER

David J Kusner, James A Barton, Kuo-Kuang Wen, Xuemin Wang, Peter A Rubenstein and Shankar S Iyer

The Journal of biological chemistry, Vol.277(52), pp.50683-50692

12/27/2002

DOI: 10.1074/jbc.M209221200

PMID: 12388543

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Abstract

Many critical cellular processes, including proliferation, vesicle trafficking, and secretion, are regulated by both phospholipase D (PLD) and the actin microfilament system. Stimulation of human PLD1 results in its association with the detergent-insoluble actin cytoskeleton, but the molecular mechanisms and functional consequences of PLD-actin interactions remain incompletely defined. Biochemical and pharmacologic modulation of actin polymerization resulted in complex bidirectional effects on PLD activity, both in vitro and in vivo. Highly purified G-actin inhibited basal and stimulated PLD activity, whereas F-actin produced the opposite effects. Actin-induced modulation of PLD activity was independent of the activating stimulus. The efficacy and potency of the effects of actin were isoform-specific but broadly conserved among actin family members. Human βγ-actin was only 45% as potent and 40% as efficacious as rabbit skeletal muscle α-actin, whereas its inhibitory profile was similar to the single actin species from the yeast, Saccharomyces cerevisiae. Use of actin polymerization-specific reagents indicated that PLD1 binds both monomeric G-actin, as well as actin filaments. These data are consistent with a model in which the physical state of the actin cytoskeleton is a critical determinant of its regulation of PLD activity.

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Title: Subtitle: Regulation of Phospholipase D Activity by Actin: ACTIN EXERTS BIDIRECTIONAL MODULATION OF MAMMALIAN PHOSPOLIPASE D ACTIVITY IN A POLYMERIZATION-DEPENDENT, ISOFORM-SPECIFIC MANNER
Creators: David J Kusner
James A Barton
Kuo-Kuang Wen
Xuemin Wang
Peter A Rubenstein
Shankar S Iyer
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.277(52), pp.50683-50692
DOI: 10.1074/jbc.M209221200
PMID: 12388543
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Language: English
Date published: 12/27/2002
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984024543202771

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