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A novel class of RanGTP binding proteins

D Görlich¹, M Dabrowski, F R Bischoff

¹Zentrum für Molekulare Biologie der Universität Heidelberg, 69120 Heidelberg, Germany. dg@mail.zmbh.uni-heidelberg.de

The Journal of Cell Biology

|July 14, 1997

Summary

Researchers discovered a new class of proteins that bind to Ran GTPase, a key regulator of nuclear transport. One protein, RanBP7, plays a role in nuclear pore complex interactions and may transport unknown cargo.

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The importin-alpha/beta complex and the GTPase Ran are crucial for nuclear protein import.
Ran's direct function was previously limited to importin-mediated nuclear import.
Ran is involved in other cellular processes like cell cycle progression.

Purpose of the Study:

To identify novel Ran targets beyond importins.
To investigate the function of RanBP7 in nuclear transport.

Main Methods:

Sequence motif analysis to identify potential Ran targets.
GTP binding assays to confirm RanGTP interactions.
Nuclear pore complex binding studies and transport assays for RanBP7.

Main Results:

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Identified approximately 20 potential Ran targets with a Ran-binding motif.
Confirmed RanGTP binding for RanBP7, RanBP8, CAS, Pse1p, Msn5p, and Cse1p.
RanBP7 inhibits Ran's GTPase activity, binds to nuclear pore complexes, and undergoes Ran-dependent bidirectional transport across the nuclear envelope.

Conclusions:

RanBP7 and related proteins represent a novel class of Ran GTPase targets.
RanBP7 may function as a nuclear transport factor for as-yet-unidentified cargo.
These findings expand the known functions of Ran in nuclear transport and cellular regulation.