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Claus Munck Petersen

GGA autoinhibition revisited

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GGA autoinhibition revisited. / Cramer, Jacob F; Gustafsen, Camilla; Behrens, Manja A; Oliveira, Cristiano L P; Pedersen, Jan Skov; Madsen, Peder; Petersen, Claus Munck; Thirup, Søren S.

In: Traffic, Vol. 11, No. 2, 2010, p. 259-73.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

APA

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MLA

Cramer, Jacob F et al. "GGA autoinhibition revisited". Traffic. 2010, 11(2). 259-73. https://doi.org/10.1111/j.1600-0854.2009.01017.x

Vancouver

Author

Cramer, Jacob F ; Gustafsen, Camilla ; Behrens, Manja A ; Oliveira, Cristiano L P ; Pedersen, Jan Skov ; Madsen, Peder ; Petersen, Claus Munck ; Thirup, Søren S. / GGA autoinhibition revisited. In: Traffic. 2010 ; Vol. 11, No. 2. pp. 259-73.

Bibtex

@article{22a237f015b311dfb95d000ea68e967b,
title = "GGA autoinhibition revisited",
abstract = "The cytosolic adaptors GGA1-3 mediate sorting of transmembrane proteins displaying a C-terminal acidic dileucine motif (DXXLL) in their cytosolic domain. GGA1 and GGA3 contain similar but intrinsic motifs that are believed to serve as autoinhibitory sites activated by the phosphorylation of a serine positioned three residues upstream of the DXXLL motif. In the present study, we have subjected the widely acknowledged concept of GGA1 autoinhibition to a thorough structural and functional examination. We find that (i) the intrinsic motif of GGA1 is inactive, (ii) only C-terminal DXXLL motifs constitute active GGA binding sites, (iii) while aspartates and phosphorylated serines one or two positions upstream of the DXXLL motif increase GGA1 binding, phosphoserines further upstream have little or no influence and (iv) phosphorylation of GGA1 does not affect its conformation or binding to Sortilin and SorLA. Taken together, our findings seem to refute the functional significance of GGA autoinhibition in particular and of intrinsic GGA binding motifs in general.",
author = "Cramer, {Jacob F} and Camilla Gustafsen and Behrens, {Manja A} and Oliveira, {Cristiano L P} and Pedersen, {Jan Skov} and Peder Madsen and Petersen, {Claus Munck} and Thirup, {S{\o}ren S}",
year = "2010",
doi = "10.1111/j.1600-0854.2009.01017.x",
language = "English",
volume = "11",
pages = "259--73",
journal = "Traffic",
issn = "1398-9219",
publisher = "Wiley-Blackwell Publishing Ltd",
number = "2",

}

RIS

TY - JOUR

T1 - GGA autoinhibition revisited

AU - Cramer, Jacob F

AU - Gustafsen, Camilla

AU - Behrens, Manja A

AU - Oliveira, Cristiano L P

AU - Pedersen, Jan Skov

AU - Madsen, Peder

AU - Petersen, Claus Munck

AU - Thirup, Søren S

PY - 2010

Y1 - 2010

N2 - The cytosolic adaptors GGA1-3 mediate sorting of transmembrane proteins displaying a C-terminal acidic dileucine motif (DXXLL) in their cytosolic domain. GGA1 and GGA3 contain similar but intrinsic motifs that are believed to serve as autoinhibitory sites activated by the phosphorylation of a serine positioned three residues upstream of the DXXLL motif. In the present study, we have subjected the widely acknowledged concept of GGA1 autoinhibition to a thorough structural and functional examination. We find that (i) the intrinsic motif of GGA1 is inactive, (ii) only C-terminal DXXLL motifs constitute active GGA binding sites, (iii) while aspartates and phosphorylated serines one or two positions upstream of the DXXLL motif increase GGA1 binding, phosphoserines further upstream have little or no influence and (iv) phosphorylation of GGA1 does not affect its conformation or binding to Sortilin and SorLA. Taken together, our findings seem to refute the functional significance of GGA autoinhibition in particular and of intrinsic GGA binding motifs in general.

AB - The cytosolic adaptors GGA1-3 mediate sorting of transmembrane proteins displaying a C-terminal acidic dileucine motif (DXXLL) in their cytosolic domain. GGA1 and GGA3 contain similar but intrinsic motifs that are believed to serve as autoinhibitory sites activated by the phosphorylation of a serine positioned three residues upstream of the DXXLL motif. In the present study, we have subjected the widely acknowledged concept of GGA1 autoinhibition to a thorough structural and functional examination. We find that (i) the intrinsic motif of GGA1 is inactive, (ii) only C-terminal DXXLL motifs constitute active GGA binding sites, (iii) while aspartates and phosphorylated serines one or two positions upstream of the DXXLL motif increase GGA1 binding, phosphoserines further upstream have little or no influence and (iv) phosphorylation of GGA1 does not affect its conformation or binding to Sortilin and SorLA. Taken together, our findings seem to refute the functional significance of GGA autoinhibition in particular and of intrinsic GGA binding motifs in general.

U2 - 10.1111/j.1600-0854.2009.01017.x

DO - 10.1111/j.1600-0854.2009.01017.x

M3 - Journal article

C2 - 20015111

VL - 11

SP - 259

EP - 273

JO - Traffic

JF - Traffic

SN - 1398-9219

IS - 2

ER -