δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function

Eric C Arakel; Kora P Richter; Anne Clancy; Blanche Schwappach

doi:10.1073/pnas.1603544113

δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function

Standard

δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function. / Arakel, Eric C; Richter, Kora P; Clancy, Anne; Schwappach, Blanche.

In: P NATL ACAD SCI USA, Vol. 113, No. 25, 21.06.2016, p. 6916-21.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Arakel, EC, Richter, KP, Clancy, A & Schwappach, B 2016, 'δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function', P NATL ACAD SCI USA, vol. 113, no. 25, pp. 6916-21. https://doi.org/10.1073/pnas.1603544113

APA

Arakel, E. C., Richter, K. P., Clancy, A., & Schwappach, B. (2016). δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function. P NATL ACAD SCI USA, 113(25), 6916-21. https://doi.org/10.1073/pnas.1603544113

Vancouver

Arakel EC, Richter KP, Clancy A, Schwappach B. δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function. P NATL ACAD SCI USA. 2016 Jun 21;113(25):6916-21. https://doi.org/10.1073/pnas.1603544113

Bibtex

@article{20401de21fb4431c9fd88f655a070a44,

title = "δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function",

abstract = "Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of δ-COP via functional complementation in yeast, we dissect the domains of the δ-COP subunit. We show that the μ-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.",

keywords = "Amino Acid Sequence, Animals, COP-Coated Vesicles/chemistry, Cattle, Sequence Homology, Amino Acid",

author = "Arakel, {Eric C} and Richter, {Kora P} and Anne Clancy and Blanche Schwappach",

year = "2016",

month = jun,

day = "21",

doi = "10.1073/pnas.1603544113",

language = "English",

volume = "113",

pages = "6916--21",

journal = "P NATL ACAD SCI USA",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "25",

}

RIS

TY - JOUR

T1 - δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function

AU - Arakel, Eric C

AU - Richter, Kora P

AU - Clancy, Anne

AU - Schwappach, Blanche

PY - 2016/6/21

Y1 - 2016/6/21

N2 - Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of δ-COP via functional complementation in yeast, we dissect the domains of the δ-COP subunit. We show that the μ-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.

AB - Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of δ-COP via functional complementation in yeast, we dissect the domains of the δ-COP subunit. We show that the μ-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.

KW - Amino Acid Sequence

KW - Animals

KW - COP-Coated Vesicles/chemistry

KW - Cattle

KW - Sequence Homology, Amino Acid

U2 - 10.1073/pnas.1603544113

DO - 10.1073/pnas.1603544113

M3 - SCORING: Journal article

C2 - 27298352

VL - 113

SP - 6916

EP - 6921

JO - P NATL ACAD SCI USA

JF - P NATL ACAD SCI USA

SN - 0027-8424

IS - 25

ER -