Open AccessWash and the wash regulatory complex function in nuclear envelope budding
Author(s) -
Jeffrey M. Verboon,
Mitsutoshi Nakamura,
Kerri Davidson,
Jacob R. Decker,
Vivek Nandakumar,
Susan M. Parkhurst
Publication year - 2020
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.243576
Subject(s) - lamin , budding , biology , nuclear lamina , microbiology and biotechnology , ran , nuclear pore , inner membrane , nuclear protein , nuclear transport , cell nucleus , nucleus , genetics , gene , transcription factor , mitochondrion
Nuclear envelope budding is a recently described phenomenon wherein large macromolecular complexes are packaged inside the nucleus and extruded through the nuclear membranes. While a general outline of the cellular events occurring during NE-budding is now in place, little is yet known about the molecular machinery and mechanisms underlying the physical aspects of NE-bud formation. Using a multidisciplinary approach, we identify Wash, its regulatory complex (SHRC), capping protein, and Arp2/3 as new molecular components involved in the physical aspects of NE-bud formation. Interestingly, Wash affects NE-budding in two ways: indirectly through general nuclear lamina disruption via an SHRC-independent interaction with Lamin B leading to inefficient NE-bud formation, and directly blocking NE-bud formation along with its SHRC, capping protein, and Arp2/3. In addition to NE-budding emerging as an important cellular process, it shares many similarities with herpesvirus nuclear egress mechanisms suggesting new avenues for exploration in both normal and disease biology.