Cloning and characterization of hSRP1γ, a tissue-specific nuclear transport factor

TY - JOUR

T1 - Cloning and characterization of hSRP1γ, a tissue-specific nuclear transport factor

AU - Nachury, Maxence V.

AU - Ryder, Ursula W.

AU - Lamond, Angus I.

AU - Weis, Karsten

PY - 1998/1/20

Y1 - 1998/1/20

N2 - Nuclear import of proteins containing a nuclear localization signal (NLS) is dependent on the presence of a cytoplasmic NLS receptor, the GTPase Ran, and p10/NTF2. The NLS receptor is a heterodimeric protein consisting of subunits of approximately 60 and 97 kDa, which have been termed importin α/β, karyopherin α/β, or PTAC 58/97. Members of the 60-kDa/importin α subunit family directly bind to the NLS motif and have been shown to function as adaptors that tether NLS-containing proteins to the p97/importin β subunit and to the downstream transport machinery. Herein we report the identification and characterization of hSRP1γ a human importin α homologue. The hSRP1γ protein is around 45% identical to the two previously identified human importin α homologues hSRP1α/Rch1 and NPI/hSRP1. hSRPIγ can form a complex with importin β and is able to mediate import of a BSA-NLS substrate in an in vitro nuclear import system. Interestingly, hSRP1γ shows a very selective expression pattern and is most abundantly expressed in skeletal muscle, representing more than 1% of the total protein in this tissue. A potential role for hSRP1γ in tissue-specific transport events is discussed.

AB - Nuclear import of proteins containing a nuclear localization signal (NLS) is dependent on the presence of a cytoplasmic NLS receptor, the GTPase Ran, and p10/NTF2. The NLS receptor is a heterodimeric protein consisting of subunits of approximately 60 and 97 kDa, which have been termed importin α/β, karyopherin α/β, or PTAC 58/97. Members of the 60-kDa/importin α subunit family directly bind to the NLS motif and have been shown to function as adaptors that tether NLS-containing proteins to the p97/importin β subunit and to the downstream transport machinery. Herein we report the identification and characterization of hSRP1γ a human importin α homologue. The hSRP1γ protein is around 45% identical to the two previously identified human importin α homologues hSRP1α/Rch1 and NPI/hSRP1. hSRPIγ can form a complex with importin β and is able to mediate import of a BSA-NLS substrate in an in vitro nuclear import system. Interestingly, hSRP1γ shows a very selective expression pattern and is most abundantly expressed in skeletal muscle, representing more than 1% of the total protein in this tissue. A potential role for hSRP1γ in tissue-specific transport events is discussed.

UR - https://www.scopus.com/pages/publications/0031882574

U2 - 10.1073/pnas.95.2.582

DO - 10.1073/pnas.95.2.582

M3 - Article

C2 - 9435235

AN - SCOPUS:0031882574

SN - 0027-8424

VL - 95

SP - 582

EP - 587

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 2

ER -