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Variable actin dynamics requirement for the exit of different cargo from the trans ‐Golgi network
Author(s) -
Lázaro-Diéguez Francisco,
Colonna Cecilia,
Cortegano Miguel,
Calvo María,
Martínez Susana E.,
Egea Gustavo
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.015
Subject(s) - fluorescence recovery after photobleaching , microbiology and biotechnology , raft , actin , golgi apparatus , actin remodeling , mdia1 , biology , actin remodeling of neurons , chemistry , actin cytoskeleton , cytoskeleton , endoplasmic reticulum , biochemistry , membrane , cell , organic chemistry , copolymer , polymer
Efficient post‐Golgi trafficking depends on microtubules, but actin filaments and actin‐associated proteins are also postulated. Here we examined, by inverse fluorescence recovery after photobleaching, the role of actin dynamics in the exit from the TGN of fluorescent‐tagged apical or basolateral and raft or non‐raft‐associated cargoes. Either the actin‐stabilizing jasplakinolide or the actin‐depolymerising latrunculin B variably but significantly inhibited post‐Golgi traffic of non‐raft associated apical p75NTR and basolateral VSV‐G cargoes. The TGN‐exit of the apical‐destined VSV‐G mutant was impaired only by latrunculin B. Strikingly, the raft‐associated GPI‐anchor protein was not affected by either actin toxin. Results indicate that actin dynamics participates in the TGN egress of both apical‐ and basolateral‐targeted proteins but is not needed for apical raft‐associated cargo.