Abstract
An emerging theme in cellular logistics is the close connection between mRNA and membrane trafficking. A prominent example is the microtubule-dependent transport of mRNAs and associated ribosomes on endosomes. This coordinated process is crucial for correct septin filamentation and efficient growth of polarised cells, such as fungal hyphae. Despite detailed knowledge on the key RNA-binding protein and the molecular motors involved, it is unclear how mRNAs are connected to membranes during transport. Here, we identify a novel factor containing a FYVE zinc finger domain for interaction with endosomal lipids and a new PAM2-like domain required for interaction with the MLLE domain of the key RNA-binding protein. Consistently, loss of this FYVE domain protein leads to specific defects in mRNA, ribosome, and septin transport without affecting general functions of endosomes or their movement. Hence, this is the first endosomal component specific for mRNP trafficking uncovering a new mechanism to couple mRNPs to endosomes.
Highlights
IntroductionImportant membranous carriers are endosomes that transport lipids, proteins, and mRNAs. Important membranous carriers are endosomes that transport lipids, proteins, and mRNAs
Trafficking of membranes is essential for intracellular logistics
In addition to the PAM2 motif (Figure 1B) and the FYVE domain, it contained five ankyrin repeats known to be protein–protein interaction interfaces (Al-Khodor et al, 2010), and a RING domain involved in ubiquitination (Figure 1A)
Summary
Important membranous carriers are endosomes that transport lipids, proteins, and mRNAs. Important membranous carriers are endosomes that transport lipids, proteins, and mRNAs These large vesicular structures are wellknown for their function in endocytosis, transporting plasma membrane proteins to their site of degradation in the lysosome/vacuole system (Huotari and Helenius, 2011; Rusten et al, 2012). They carry out other functions, such as receptor recycling or cytoplasmic signalling, and are considered to be multipurpose platforms (Gould and Lippincott-Schwartz, 2009). These lipids are recognised by distinct protein domains, such as the FYVE zinc finger (Stenmark et al, 1996)
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