The association of Xenopus nuclear factor 7 with subcellular structures is dependent upon phosphorylation and specific domains

Xiaoxia Li, Weinian Shou, Malgorzata Kloc, Bramham A. Reddy, Laurence D. Etkin

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The function of proteins is often regulated by their association with specific subcellular structures. Xenopus nuclear factor 7 (xnf7) is a putative transcription factor that is selectively retained in the cytoplasm from fertilization through the mid blastula transition (MBT). Cytoplasmic retention is dependent upon the presence of a 22-amino-acid cytoplasmic retention domain and the phosphorylation of two sites (site 1 and site 2) within the protein. We show that the N-terminal acidic domain of xnf7 transactivated a reporter gene in transfected cells, supporting its function as a transcription factor. During mitosis xnf7 was associated with the mitotic spindle and chromosomes, while during the short embryonic interphase it was associated with structures at the poles which were most likely centrosomes. The association with these structures was dependent upon the presence of protein domains and the phosphorylation of a specific phosphorylation site (site 2). In addition, we determined that association with the spindle or centrosomes was not necessary for cytoplasmic retention prior to the MBT. We suggest that the association of xnf7 with these structures is due to its interaction with other proteins that are colocalized.

Original languageEnglish (US)
Pages (from-to)473-481
Number of pages9
JournalExperimental Cell Research
Volume213
Issue number2
DOIs
StatePublished - 1994
Externally publishedYes

Fingerprint

Phosphorylation
Blastula
Centrosome
Transcription Factors
Spindle Apparatus
Proteins
Interphase
Reporter Genes
Mitosis
Fertilization
Cytoplasm
Chromosomes
Amino Acids
Xenopus XNF7 protein

ASJC Scopus subject areas

  • Cell Biology

Cite this

The association of Xenopus nuclear factor 7 with subcellular structures is dependent upon phosphorylation and specific domains. / Li, Xiaoxia; Shou, Weinian; Kloc, Malgorzata; Reddy, Bramham A.; Etkin, Laurence D.

In: Experimental Cell Research, Vol. 213, No. 2, 1994, p. 473-481.

Research output: Contribution to journalArticle

Li, Xiaoxia ; Shou, Weinian ; Kloc, Malgorzata ; Reddy, Bramham A. ; Etkin, Laurence D. / The association of Xenopus nuclear factor 7 with subcellular structures is dependent upon phosphorylation and specific domains. In: Experimental Cell Research. 1994 ; Vol. 213, No. 2. pp. 473-481.
@article{2070623baa9741179f7b6e622d0753bb,
title = "The association of Xenopus nuclear factor 7 with subcellular structures is dependent upon phosphorylation and specific domains",
abstract = "The function of proteins is often regulated by their association with specific subcellular structures. Xenopus nuclear factor 7 (xnf7) is a putative transcription factor that is selectively retained in the cytoplasm from fertilization through the mid blastula transition (MBT). Cytoplasmic retention is dependent upon the presence of a 22-amino-acid cytoplasmic retention domain and the phosphorylation of two sites (site 1 and site 2) within the protein. We show that the N-terminal acidic domain of xnf7 transactivated a reporter gene in transfected cells, supporting its function as a transcription factor. During mitosis xnf7 was associated with the mitotic spindle and chromosomes, while during the short embryonic interphase it was associated with structures at the poles which were most likely centrosomes. The association with these structures was dependent upon the presence of protein domains and the phosphorylation of a specific phosphorylation site (site 2). In addition, we determined that association with the spindle or centrosomes was not necessary for cytoplasmic retention prior to the MBT. We suggest that the association of xnf7 with these structures is due to its interaction with other proteins that are colocalized.",
author = "Xiaoxia Li and Weinian Shou and Malgorzata Kloc and Reddy, {Bramham A.} and Etkin, {Laurence D.}",
year = "1994",
doi = "10.1006/excr.1994.1225",
language = "English (US)",
volume = "213",
pages = "473--481",
journal = "Experimental Cell Research",
issn = "0014-4827",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - The association of Xenopus nuclear factor 7 with subcellular structures is dependent upon phosphorylation and specific domains

AU - Li, Xiaoxia

AU - Shou, Weinian

AU - Kloc, Malgorzata

AU - Reddy, Bramham A.

AU - Etkin, Laurence D.

PY - 1994

Y1 - 1994

N2 - The function of proteins is often regulated by their association with specific subcellular structures. Xenopus nuclear factor 7 (xnf7) is a putative transcription factor that is selectively retained in the cytoplasm from fertilization through the mid blastula transition (MBT). Cytoplasmic retention is dependent upon the presence of a 22-amino-acid cytoplasmic retention domain and the phosphorylation of two sites (site 1 and site 2) within the protein. We show that the N-terminal acidic domain of xnf7 transactivated a reporter gene in transfected cells, supporting its function as a transcription factor. During mitosis xnf7 was associated with the mitotic spindle and chromosomes, while during the short embryonic interphase it was associated with structures at the poles which were most likely centrosomes. The association with these structures was dependent upon the presence of protein domains and the phosphorylation of a specific phosphorylation site (site 2). In addition, we determined that association with the spindle or centrosomes was not necessary for cytoplasmic retention prior to the MBT. We suggest that the association of xnf7 with these structures is due to its interaction with other proteins that are colocalized.

AB - The function of proteins is often regulated by their association with specific subcellular structures. Xenopus nuclear factor 7 (xnf7) is a putative transcription factor that is selectively retained in the cytoplasm from fertilization through the mid blastula transition (MBT). Cytoplasmic retention is dependent upon the presence of a 22-amino-acid cytoplasmic retention domain and the phosphorylation of two sites (site 1 and site 2) within the protein. We show that the N-terminal acidic domain of xnf7 transactivated a reporter gene in transfected cells, supporting its function as a transcription factor. During mitosis xnf7 was associated with the mitotic spindle and chromosomes, while during the short embryonic interphase it was associated with structures at the poles which were most likely centrosomes. The association with these structures was dependent upon the presence of protein domains and the phosphorylation of a specific phosphorylation site (site 2). In addition, we determined that association with the spindle or centrosomes was not necessary for cytoplasmic retention prior to the MBT. We suggest that the association of xnf7 with these structures is due to its interaction with other proteins that are colocalized.

UR - http://www.scopus.com/inward/record.url?scp=0028109030&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028109030&partnerID=8YFLogxK

U2 - 10.1006/excr.1994.1225

DO - 10.1006/excr.1994.1225

M3 - Article

C2 - 8050504

AN - SCOPUS:0028109030

VL - 213

SP - 473

EP - 481

JO - Experimental Cell Research

JF - Experimental Cell Research

SN - 0014-4827

IS - 2

ER -