TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells: In the reproductive organs and in the brain of the imago

Marianna Pintér, Gáspár Jékely, Robert J. Szepesi, Attila Farkas, Ulrich Theopold, Helmut E. Meyer, Dan Lindholm, Dick R. Nässel, Dan Hultmark, P. Friedrich

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

We have cloned a Drosophila homolog of the membrane fusion protein CDC48/p97. The open reading frame of the Drosophila homolog encodes an 801 amino acid long protein (TER94), which shows high similarity to the known CDC48/p97 sequences. The chromosomal position of TER94 is 46 C/D. TER94 is expressed in embryo, in pupae and in imago, but is suppressed in larva. In the imago, the immunoreactivity was exclusively present in the head and in the gonads of both sexes. In the head the most striking staining was observed in the entire neuropil of the mushroom body and in the antennal glomeruli. Besides TER94, sex-specific forms were also detected in the gonads of the imago: p47 in the ovaries and p98 in the testis. TER94/p47 staining was observed in the nurse cells and often in the oocytes, while TER94/p98 staining was present in the sperm bundles. On the basis of its distribution we suggest that TER94 functions in the protein transport utilizing endoplasmic reticulum and Golgi derived vesicles.

Original languageEnglish
Pages (from-to)91-98
Number of pages8
JournalInsect Biochemistry and Molecular Biology
Volume28
Issue number2
DOIs
Publication statusPublished - Feb 1998

Fingerprint

Membrane Fusion Proteins
imagos
Drosophila
gonads
Brain
Gonads
Staining and Labeling
brain
Head
Mushroom Bodies
mushroom bodies
Pupa
Proteins
Neuropil
protein transport
proteins
gender
Protein Transport
cells
nurses

Keywords

  • CAP, Ca-activated protease
  • ER, endoplasmic reticulum
  • GA, Golgi apparatus
  • GST, glutathione S-transferase
  • NSF, N-ethylmaleimid sensitive factor
  • PBS, phosphate buffered saline
  • SDS-PAGE, sodium dodecylsulfate polyacrylamide gelelectrophoresis
  • TER, transient endoplasmic reticulum

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry

Cite this

TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells : In the reproductive organs and in the brain of the imago. / Pintér, Marianna; Jékely, Gáspár; Szepesi, Robert J.; Farkas, Attila; Theopold, Ulrich; Meyer, Helmut E.; Lindholm, Dan; Nässel, Dick R.; Hultmark, Dan; Friedrich, P.

In: Insect Biochemistry and Molecular Biology, Vol. 28, No. 2, 02.1998, p. 91-98.

Research output: Contribution to journalArticle

Pintér, Marianna ; Jékely, Gáspár ; Szepesi, Robert J. ; Farkas, Attila ; Theopold, Ulrich ; Meyer, Helmut E. ; Lindholm, Dan ; Nässel, Dick R. ; Hultmark, Dan ; Friedrich, P. / TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells : In the reproductive organs and in the brain of the imago. In: Insect Biochemistry and Molecular Biology. 1998 ; Vol. 28, No. 2. pp. 91-98.
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abstract = "We have cloned a Drosophila homolog of the membrane fusion protein CDC48/p97. The open reading frame of the Drosophila homolog encodes an 801 amino acid long protein (TER94), which shows high similarity to the known CDC48/p97 sequences. The chromosomal position of TER94 is 46 C/D. TER94 is expressed in embryo, in pupae and in imago, but is suppressed in larva. In the imago, the immunoreactivity was exclusively present in the head and in the gonads of both sexes. In the head the most striking staining was observed in the entire neuropil of the mushroom body and in the antennal glomeruli. Besides TER94, sex-specific forms were also detected in the gonads of the imago: p47 in the ovaries and p98 in the testis. TER94/p47 staining was observed in the nurse cells and often in the oocytes, while TER94/p98 staining was present in the sperm bundles. On the basis of its distribution we suggest that TER94 functions in the protein transport utilizing endoplasmic reticulum and Golgi derived vesicles.",
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