Arabidopsis 56-amino acid serine palmitoyltransferase- interacting proteins stimulate sphingolipid synthesis, are essential, and affect mycotoxin sensitivity

Athen N. Kimberlin, Saurav Majumder, Gongshe Han, Ming Chen, Rebecca E. Cahoon, Julie M. Stone, Teresa M. Dunn, Edgar B. Cahoona

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Maintenance of sphingolipid homeostasis is critical for cell growth and programmed cell death (PCD). Serine palmitoyltransferase (SPT), composed of LCB1 and LCB2 subunits, catalyzes the primary regulatory point for sphingolipid synthesis. Small subunits of SPT (ssSPT) that strongly stimulate SPT activity have been identified in mammals, but the role of ssSPT in eukaryotic cells is unclear. Candidate Arabidopsis thaliana ssSPTs, ssSPTa and ssSPTb, were identified and characterized. Expression of these 56-amino acid polypeptides in a Saccharomyces cerevisiae SPT null mutant stimulated SPT activity from the Arabidopsis LCB1/LCB2 heterodimer by >100-fold through physical interaction with LCB1/LCB2. ssSPTa transcripts were more enriched in all organs and >400-fold more abundant in pollen than ssSPTb transcripts. Accordingly, homozygous ssSPTa T-DNA mutants were not recoverable, and 50% nonviable pollen was detected in heterozygous ssspta mutants. Pollen viability was recovered by expression of wild-type ssSPTa or ssSPTb under control of the ssSPTa promoter, indicating ssSPTa and ssSPTb functional redundancy. SPT activity and sensitivity to the PCD-inducing mycotoxin fumonisin B1 (FB1) were increased by ssSPTa overexpression. Conversely, SPT activity and FB1 sensitivity were reduced in ssSPTa RNA interference lines. These results demonstrate that ssSPTs are essential for male gametophytes, are important for FB1 sensitivity, and limit sphingolipid synthesis in planta.

Original languageEnglish (US)
Pages (from-to)4627-4639
Number of pages13
JournalPlant Cell
Volume25
Issue number11
DOIs
StatePublished - Nov 1 2013

Fingerprint

serine C-palmitoyltransferase
Serine C-Palmitoyltransferase
sphingolipids
Sphingolipids
Mycotoxins
Arabidopsis
mycotoxins
Amino Acids
amino acids
fumonisin B1
synthesis
Proteins
proteins
pollen
Pollen
mutants
apoptosis
gametophytes
Plantae
RNA interference

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

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Arabidopsis 56-amino acid serine palmitoyltransferase- interacting proteins stimulate sphingolipid synthesis, are essential, and affect mycotoxin sensitivity. / Kimberlin, Athen N.; Majumder, Saurav; Han, Gongshe; Chen, Ming; Cahoon, Rebecca E.; Stone, Julie M.; Dunn, Teresa M.; Cahoona, Edgar B.

In: Plant Cell, Vol. 25, No. 11, 01.11.2013, p. 4627-4639.

Research output: Contribution to journalArticle

Kimberlin, Athen N. ; Majumder, Saurav ; Han, Gongshe ; Chen, Ming ; Cahoon, Rebecca E. ; Stone, Julie M. ; Dunn, Teresa M. ; Cahoona, Edgar B. / Arabidopsis 56-amino acid serine palmitoyltransferase- interacting proteins stimulate sphingolipid synthesis, are essential, and affect mycotoxin sensitivity. In: Plant Cell. 2013 ; Vol. 25, No. 11. pp. 4627-4639.
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T1 - Arabidopsis 56-amino acid serine palmitoyltransferase- interacting proteins stimulate sphingolipid synthesis, are essential, and affect mycotoxin sensitivity

AU - Kimberlin, Athen N.

AU - Majumder, Saurav

AU - Han, Gongshe

AU - Chen, Ming

AU - Cahoon, Rebecca E.

AU - Stone, Julie M.

AU - Dunn, Teresa M.

AU - Cahoona, Edgar B.

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