Evolutionary conservation of physical and functional interactions between phospholipase D and actin

Kusner, David J.; Barton, James A.; Qin, Chunbo; Wang, Xuemin; Iyer, Shankar S.

doi:10.1016/s0003-9861(03)00052-3

Cited by 64 publications

(60 citation statements)

References 47 publications

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“…In contrast, monomeric G-actin inhibits PLD activity in a species-specific manner (22) in that, in vitro, G-actin-induced PLD inhibition is 20-fold greater for human PLD1 than it is for Streptomyces PLD (23). The greatest degree of inhibition occurs upon the initiation of PLD activity in the presence of G-actin; less inhibition is observed when G-actin is added to previously activated PLD (23). Phosphatidylinositol 4,5-bisphosphate is a required cofactor in human PLD activity; in contrast, bacterial PLD activity does not exhibit a cofactor requirement.…”

Section: Discussionmentioning

confidence: 97%

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Gonococcal Phospholipase D Modulates the Expression and Function of Complement Receptor 3 in Primary Cervical Epithelial Cells

2003

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CR3-mediated endocytosis is a primary mechanism by which Neisseria gonorrhoeae elicits membrane ruffling and cellular invasion of the cervical epithelia. Our data indicate that, upon infection of cervical epithelia, N. gonorrhoeae specifically releases proteins, including a phospholipase D (PLD) homolog, which facilitate membrane ruffling. To elucidate the function of gonococcal PLD in infection of the cervical epithelia, we constructed an N. gonorrhoeae PLD mutant. By comparative association and/or invasion assays, we demonstrated that PLD mutant gonococci are impaired in their ability to adhere to and to invade primary cervical cells. This defect can be rescued by the addition of supernatants obtained from wild-type-infected cell monolayers but not by exogenously added Streptomyces PLD. The decreased level of total cell association (i.e., adherence and invasion) observed for mutant gonococci is, in part, attributed to the inability of these bacteria to recruit CR3 to the cervical cell surface with extended infection. Using electron microscopy, we demonstrate that gonococcal PLD may be necessary to potentiate membrane ruffling and clustering of gonococci on the cervical cell surface. These data may be indicative of the inability of PLD mutant gonococci to recruit CR3 to the cervical cell surface. Alternatively, in the absence of gonococcal PLD, signal transduction events required for CR3 clustering may not be activated. Collectively, our data indicate that PLD augments CR3-mediated gonococcus invasion of and survival within cervical epithelia.Neisseria gonorrhoeae is a strict human pathogen, which causes the sexually transmitted disease gonorrhea. This organism possesses multiple mechanisms by which it is able to colonize its sole human host and which are dependent upon the particular microenvironment of the infection site. In this respect, the gonococcus senses its particular microenvironment and adjusts its mode of pathogenicity accordingly. Several gonococcal constituents are implicated to play a role in its pathogenicity, including lipooligosaccharide (LOS), porin, pilus, and the opacity-associated outer membrane proteins. Invasion of male urethral epithelial cells is mediated by LOS, the terminal galactose of which serves as a ligand for the asialoglycoprotein receptor (ASGP-R) (15). An intimate association between the gonococcal and host cell membranes precedes clathrin-dependent endocytosis (15). In contrast, complement (CЈ) receptor type 3 (CR3)-mediated endocytosis is a primary mechanism by which N. gonorrhoeae invades primary human cervical epithelial cells (8). This process is dependent upon the cooperative binding of (gonococcus-bound, host-derived) iC3b, gonococcal porin, and gonococcal pilus to the I domain of CR3 (7, 9). Engagement of CR3 results in membrane ruffling (8) and internalization of gonococci in macropinosomes (10).Our studies show that ruffling induced by gonococci during cervical cell infection is delayed from the onset of infection by 60 to 90 min (10). The onset of ruffling can be ...

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Section: Discussionmentioning

confidence: 97%

“…Bacterial, plant, and human PLDs directly bind polymeric F-actin, which in turn increases PLD activity (23). In contrast, monomeric G-actin inhibits PLD activity in a species-specific manner (22) in that, in vitro, G-actin-induced PLD inhibition is 20-fold greater for human PLD1 than it is for Streptomyces PLD (23).…”

Section: Discussionmentioning

confidence: 99%

Gonococcal Phospholipase D Modulates the Expression and Function of Complement Receptor 3 in Primary Cervical Epithelial Cells

2003

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“…AtPLDa1 in Arabidopsis was detected in the plasma membrane, intracellular membranes, mitochondria, and clathrin-coated vesicles (Fan et al, 1999). AtPLDb1 was reported to bind actin in vitro, which is a major component of a microfilament in the cells (Kusner et al, 2003). showed that the fusion protein of tomato LePLDb1 and GFP was detected in the cytosol of cultured cells, whereas treatment with xylanase elicitor induced the relocalization to punctate structures within the cytosol.…”

Section: Possible Mechanisms For the Different Functions Of Pld Isoformsmentioning

confidence: 99%

Suppression of a Phospholipase D Gene,OsPLDβ1, Activates Defense Responses and Increases Disease Resistance in Rice

et al. 2009

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Phospholipase D (PLD) plays an important role in plants, including responses to abiotic as well as biotic stresses. A survey of the rice (Oryza sativa) genome database indicated the presence of 17 PLD genes in the genome, among which OsPLDa1, OsPLDa5, and OsPLDb1 were highly expressed in most tissues studied. To examine the physiological function of PLD in rice, we made knockdown plants for each PLD isoform by introducing gene-specific RNA interference constructs. One of them, OsPLDb1-knockdown plants, showed the accumulation of reactive oxygen species in the absence of pathogen infection. Reverse transcription-polymerase chain reaction and DNA microarray analyses revealed that the knockdown of OsPLDb1 resulted in the up-/down-regulation of more than 1,400 genes, including the induction of defense-related genes such as pathogenesis-related protein genes and WRKY/ERF family transcription factor genes. Hypersensitive response-like cell death and phytoalexin production were also observed at a later phase of growth in the OsPLDb1-knockdown plants. These results indicated that the OsPLDb1-knockdown plants spontaneously activated the defense responses in the absence of pathogen infection. Furthermore, the OsPLDb1-knockdown plants exhibited increased resistance to the infection of major pathogens of rice, Pyricularia grisea and Xanthomonas oryzae pv oryzae. These results suggested that OsPLDb1 functions as a negative regulator of defense responses and disease resistance in rice.

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“…PLDα1, the predominant PLD, is responsible for the common PLD activity in Arabidopsis, and is involved in ABA and ethylene signal transduction, freezing tolerance and wound-induced JA accumulation [13]. PLDβ1 can bind to α-actin in vitro [40], and its expression is induced by wound stress [25]. PLDδ is activated by oleic acid and is closely associated with the microtubule cytoskeleton and plasma membrane.…”

Section: Introductionmentioning

confidence: 99%

Genome-wide analysis of the phospholipase D family in Oryza sativa and functional characterization of PLDβ1 in seed germination

2007

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npg Phospholipase D (PLD) plays a critical role in plant growth and development, as well as in hormone and stress responses. PLD encoding genes constitute a large gene family that are present in higher plants. There are 12 members of the PLD family in Arabidopsis thaliana and several of them have been functionally characterized; however, the members of the PLD family in Oryza sativa remain to be fully described. Through genome-wide analysis, 17 PLD members found in different chromosomes have been identified in rice. Protein domain structural analysis reveals a novel subfamily, besides the C2-PLDs and PXPH-PLDs, that is present in rice -the SP-PLD. SP-PLD harbors a signal peptide instead of the C2 or PXPH domains at the N-terminus. Expression pattern analysis indicates that most PLD-encoding genes are differentially expressed in various tissues, or are induced by hormones or stress conditions, suggesting the involvement of PLD in multiple developmental processes. Transgenic studies have shown that the suppressed expression of rice PLDβ1 results in reduced sensitivity to exogenous ABA during seed germination. Further analysis of the expression of ABA signaling-related genes has revealed that PLDβ1 stimulates ABA signaling by activating SAPK, thus repressing GAmyb expression and inhibiting seed germination.

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Evolutionary conservation of physical and functional interactions between phospholipase D and actin

Cited by 64 publications

References 47 publications

Gonococcal Phospholipase D Modulates the Expression and Function of Complement Receptor 3 in Primary Cervical Epithelial Cells

Gonococcal Phospholipase D Modulates the Expression and Function of Complement Receptor 3 in Primary Cervical Epithelial Cells

Suppression of a Phospholipase D Gene,OsPLDβ1, Activates Defense Responses and Increases Disease Resistance in Rice

Genome-wide analysis of the phospholipase D family in Oryza sativa and functional characterization of PLDβ1 in seed germination

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